메뉴 건너뛰기




Volumn 75, Issue 2, 2011, Pages 321-360

Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers

Author keywords

[No Author keywords available]

Indexed keywords

3,4 DIHYDROXY 2 BUTANONE 4 PHOSPHATE SYNTHASE; 5 AMINO 6 RIBITYLAMINO 2,4 PYRIMIDINEDIONE 5' PHOSPHATE; ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; COBAMAMIDE; DEAMINASE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; FLAVINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE II; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE III; HYDROLASE; LUMAZINE; LUMAZINE SYNTHASE; OXIDOREDUCTASE; RIBOFLAVIN; RIBOFLAVIN KINASE; RIBOFLAVIN SYNTHASE; SULFONAMIDE; UNCLASSIFIED DRUG;

EID: 79958022433     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00030-10     Document Type: Review
Times cited : (289)

References (560)
  • 2
    • 0020024605 scopus 로고
    • FMN phosphatase and FAD pyrophosphatase in rat intestinal brush borders: Role in intestinal absorption of dietary riboflavin
    • Akiyama, T., J. Selhub, and I. H. Rosenberg. 1982. FMN phosphatase and FAD pyrophosphatase in rat intestinal brush borders: role in intestinal absorption of dietary riboflavin. J. Nutr. 112:263-268.
    • (1982) J. Nutr. , vol.112 , pp. 263-268
    • Akiyama, T.1    Selhub, J.2    Rosenberg, I.H.3
  • 5
    • 77953525125 scopus 로고    scopus 로고
    • A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance
    • Asai, S., K. Mase, and H. Yoshioka. 2010. A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance. Plant J. 62:911-924.
    • (2010) Plant J. , vol.62 , pp. 911-924
    • Asai, S.1    Mase, K.2    Yoshioka, H.3
  • 6
    • 0032254388 scopus 로고    scopus 로고
    • Formation and distribution of modified FAD between isozymes of alcohol oxidase in the methylotrophic yeast Pichia methanolica
    • Moscow
    • Ashin, V. V., and Y. A. Trotsenko. 1998. Formation and distribution of modified FAD between isozymes of alcohol oxidase in the methylotrophic yeast Pichia methanolica. Biochemistry (Moscow) 63:1407-1413.
    • (1998) Biochemistry , vol.63 , pp. 1407-1413
    • Ashin, V.V.1    Trotsenko, Y.A.2
  • 7
    • 73649191856 scopus 로고
    • Studies on the biosynthesis of riboflavin. 7. The incorporation of adenine and guanine into riboflavin and into nucleic acid purines in Eremothecium ashbyii and Candida flareri
    • Audley, B. G., and T. W. Goodwin. 1962. Studies on the biosynthesis of riboflavin. 7. The incorporation of adenine and guanine into riboflavin and into nucleic acid purines in Eremothecium ashbyii and Candida flareri. Biochem. J. 84:587-592.
    • (1962) Biochem. J. , vol.84 , pp. 587-592
    • Audley, B.G.1    Goodwin, T.W.2
  • 9
    • 27644585876 scopus 로고
    • Selection and some properties of the mutants rib81 with impaired regulation of riboflavin biosynthesis
    • In Russian
    • Babyak, L. Y., A. A. Sibirnyi, and G. M. Shavlovskii. 1993. Selection and some properties of the mutants rib81 with impaired regulation of riboflavin biosynthesis. Tsitol. Genet. 27:28-32. (In Russian.)
    • (1993) Tsitol. Genet. , vol.27 , pp. 28-32
    • Babyak, L.Y.1    Sibirnyi, A.A.2    Shavlovskii, G.M.3
  • 10
    • 0001449413 scopus 로고
    • Biosynthesis of flavins
    • F. Müller (ed.), CRC Press, Boca Raton, FL
    • Bacher, A. 1991. Biosynthesis of flavins, p. 215-249. In F. Müller (ed.), Chemistry and biochemistry of flavoenzymes, vol. 1. CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.1 , pp. 215-249
    • Bacher, A.1
  • 11
    • 79958030881 scopus 로고
    • Riboflavin synthases of Bacillus subtilis
    • T. P. Singer (ed.), Elsevier, Amsterdam, Netherlands
    • Bacher, A., R. Bauer, U. Eggers, H. Harders, and H. Schnepple. 1976. Riboflavin synthases of Bacillus subtilis, p. 729-732. In T. P. Singer (ed.), Flavins and flavoproteins. Elsevier, Amsterdam, Netherlands.
    • (1976) Flavins and Flavoproteins , pp. 729-732
    • Bacher, A.1    Bauer, R.2    Eggers, U.3    Harders, H.4    Schnepple, H.5
  • 12
    • 0018827587 scopus 로고
    • Riboflavin synthases of Bacillus subtilis. Purification and properties
    • Bacher, A., et al. 1980. Riboflavin synthases of Bacillus subtilis. Purification and properties. J. Biol. Chem. 255:632-637.
    • (1980) J. Biol. Chem. , vol.255 , pp. 632-637
    • Bacher, A.1
  • 13
    • 0035235055 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin
    • Bacher, A., et al. 2001. Biosynthesis of riboflavin. Vitam. Horm. 61:1-49.
    • (2001) Vitam. Horm. , vol.61 , pp. 1-49
    • Bacher, A.1
  • 16
    • 0014962796 scopus 로고
    • Biosynthesis of riboflavin. Formation of 2,5-diamino-6-hydroxy- 4(1′-D-ribitylamino)pyrimidine in riboflavin auxotroph
    • Bacher, A., and F. Lingens. 1970. Biosynthesis of riboflavin. Formation of 2,5-diamino-6-hydroxy-4(1′-D-ribitylamino)pyrimidine in riboflavin auxotroph. J. Biol. Chem. 245:4647-4652.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4647-4652
    • Bacher, A.1    Lingens, F.2
  • 17
    • 0015240352 scopus 로고
    • Biosynthesis of riboflavin. Formation of 6-hydroxy-2,4,5- triaminopyrimidine in RIB7 mutants of Saccharomyces cerevisiae
    • Bacher, A., and F. Lingens. 1971. Biosynthesis of riboflavin. Formation of 6-hydroxy-2,4,5-triaminopyrimidine in RIB7 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 246:7018-7022.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7018-7022
    • Bacher, A.1    Lingens, F.2
  • 18
    • 0015901054 scopus 로고
    • Biosynthesis of riboflavin. The structure of the purine precursor
    • Bacher, A., and B. Mailander. 1973. Biosynthesis of riboflavin. The structure of the purine precursor. J. Biol. Chem. 248:6227-6231.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6227-6231
    • Bacher, A.1    Mailander, B.2
  • 19
    • 0018138558 scopus 로고
    • Biosynthesis of riboflavin in Bacillus subtilis: Function and genetic control of the riboflavin synthase complex
    • Bacher, A., and B. Mailander. 1978. Biosynthesis of riboflavin in Bacillus subtilis: function and genetic control of the riboflavin synthase complex. J. Bacteriol. 134:476-482. (Pubitemid 8331159)
    • (1978) Journal of Bacteriology , vol.134 , Issue.2 , pp. 476-482
    • Bacher, A.1    Mailaender, B.2
  • 20
    • 0000588953 scopus 로고
    • Biosynthesis of flavins
    • H. Dugas and F. P. Schmidtchen (ed.), Springer Verlag, Berlin, Germany
    • Bacher, A., et al. 1993. Biosynthesis of flavins, p. 147-192. In H. Dugas and F. P. Schmidtchen (ed.), Bioorganic chemistry frontiers. Springer Verlag, Berlin, Germany.
    • (1993) Bioorganic Chemistry Frontiers , pp. 147-192
    • Bacher, A.1
  • 22
    • 0347683482 scopus 로고    scopus 로고
    • Riboflavin uptake and FAD synthesis in Saccharomyces cerevisiae mitochondria: Involvement of the Flx1p carrier in FAD export
    • Bafunno, V., et al. 2004. Riboflavin uptake and FAD synthesis in Saccharomyces cerevisiae mitochondria: involvement of the Flx1p carrier in FAD export. J. Biol. Chem. 279:95-102.
    • (2004) J. Biol. Chem. , vol.279 , pp. 95-102
    • Bafunno, V.1
  • 24
    • 0030721976 scopus 로고    scopus 로고
    • Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver - The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
    • Barile, M., et al. 1997. Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver - the occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria. Eur. J. Biochem. 249:777-785.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 777-785
    • Barile, M.1
  • 25
    • 46349083026 scopus 로고    scopus 로고
    • The distributions, mechanisms, and structures of metabolite-binding riboswitches
    • Barrick, J. E., and R. R. Breaker. 2007. The distributions, mechanisms, and structures of metabolite-binding riboswitches. Genome Biol. 8:R239.
    • (2007) Genome Biol. , vol.8
    • Barrick, J.E.1    Breaker, R.R.2
  • 26
    • 0037424602 scopus 로고    scopus 로고
    • Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold
    • Bauer, S., et al. 2003. Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. J. Mol. Biol. 326:1463-1473.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1463-1473
    • Bauer, S.1
  • 27
    • 0014528989 scopus 로고
    • Biosynthesis of riboflavine in Corynebacterium species: The purine precursor
    • Baugh, C. M., and C. L. Krumdieck. 1969. Biosynthesis of riboflavine in Corynebacterium species: the purine precursor. J. Bacteriol. 98:1114-1119.
    • (1969) J. Bacteriol. , vol.98 , pp. 1114-1119
    • Baugh, C.M.1    Krumdieck, C.L.2
  • 28
    • 0014578214 scopus 로고
    • The formation of riboflavin from 6,7-dimethyl-8-ribityllumazine in acid media
    • Beach, R., and G. W. Plaut. 1969. The formation of riboflavin from 6,7-dimethyl-8-ribityllumazine in acid media. Tetrahedron Lett. 40:3489-3492.
    • (1969) Tetrahedron Lett. , vol.40 , pp. 3489-3492
    • Beach, R.1    Plaut, G.W.2
  • 29
    • 0014934697 scopus 로고
    • Stereospecificity of the enzymatic synthesis of the o-xylene ring of riboflavin
    • Beach, R. L., and G. W. Plaut. 1970. Stereospecificity of the enzymatic synthesis of the o-xylene ring of riboflavin. J. Am. Chem. Soc. 92:2913-2916.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 2913-2916
    • Beach, R.L.1    Plaut, G.W.2
  • 30
    • 0038707365 scopus 로고
    • Flavin coenzymes
    • P. Boyer, H. Lardy, and K. Myrback (ed.), Academic Pres, New York, NY
    • Beinert, H. 1960. Flavin coenzymes, p. 339-416. In P. Boyer, H. Lardy, and K. Myrback (ed.), The enzymes, vol. 2. Academic Pres, New York, NY.
    • (1960) The Enzymes , vol.2 , pp. 339-416
    • Beinert, H.1
  • 31
    • 0004024282 scopus 로고    scopus 로고
    • 2nd ed., Cambridge University Press, Cambridge, United Kingdom
    • Bender, D. A. 2003. Nutritional biochemistry of the vitamins, 2nd ed., p. 172-199. Cambridge University Press, Cambridge, United Kingdom.
    • (2003) Nutritional Biochemistry of the Vitamins , pp. 172-199
    • Bender, D.A.1
  • 32
    • 0031968623 scopus 로고    scopus 로고
    • Hemolytic properties and riboflavin synthesis of Helicobacter pylori: Cloning and functional characterization of the ribA gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli
    • Bereswill, S., et al. 1998. Hemolytic properties and riboflavin synthesis of Helicobacter pylori: cloning and functional characterization of the ribA gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli. Med. Microbiol. Immunol. 186:177-187.
    • (1998) Med. Microbiol. Immunol. , vol.186 , pp. 177-187
    • Bereswill, S.1
  • 33
  • 34
    • 0001120822 scopus 로고
    • Industrial products of biotechnology: Application of gene technology
    • H. J. Rehm and G. Reed (ed.), VCH, Weinheim, Germany
    • Bigelis, R. 1989. Industrial products of biotechnology: application of gene technology, p. 243. In H. J. Rehm and G. Reed (ed.), Biotechnology, vol. 7b. VCH, Weinheim, Germany.
    • (1989) Biotechnology , vol.7 B , pp. 243
    • Bigelis, R.1
  • 36
    • 33845700514 scopus 로고    scopus 로고
    • Riboswitches as antibacterial drug targets
    • Blount, K. F., and R. R. Breaker. 2006. Riboswitches as antibacterial drug targets. Nat. Biotechnol. 24:1558-1564.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1558-1564
    • Blount, K.F.1    Breaker, R.R.2
  • 37
    • 77949677235 scopus 로고    scopus 로고
    • An atypical riboflavin pathway is essential for Brucella abortus virulence
    • Bonomi, H. R., et al. 2010. An atypical riboflavin pathway is essential for Brucella abortus virulence. PLoS One 5:e9435.
    • (2010) PLoS One , vol.5
    • Bonomi, H.R.1
  • 38
    • 19544393194 scopus 로고    scopus 로고
    • Positive selection of mutants defective in transcriptional repression of riboflavin synthesis by iron in the flavinogenic yeast Pichia guilliermondii
    • DOI 10.1016/j.femsyr.2005.03.007, PII S1567135605000668
    • Boretsky, Y. R., et al. 2005. Positive selection of mutants defective in transcriptional repression of riboflavin synthesis by iron in the flavinogenic yeast Pichia guilliermondii. FEMS Yeast Res. 5:829-837. (Pubitemid 40733229)
    • (2005) FEMS Yeast Research , vol.5 , Issue.9 , pp. 829-837
    • Boretsky, Y.R.1    Kapustyak, K.Y.2    Fayura, L.R.3    Stasyk, O.V.4    Stenchuk, M.M.5    Bobak, Y.P.6    Drobot, L.B.7    Sibirny, A.A.8
  • 39
    • 35548966025 scopus 로고    scopus 로고
    • Mutations and environmental factors affecting regulation of riboflavin synthesis and iron assimilation also cause oxidative stress in the yeast Pichia guilliermondii
    • DOI 10.1002/jobm.200610279
    • Boretsky, Y. R., et al. 2007. Mutations and environmental factors affecting regulation of riboflavin synthesis and iron assimilation also cause oxidative stress in the yeast Pichia guilliermondii. J. Basic Microbiol. 47:371-377. (Pubitemid 350003890)
    • (2007) Journal of Basic Microbiology , vol.47 , Issue.5 , pp. 371-377
    • Boretsky, Y.R.1    Protchenko, O.V.2    Prokopiv, T.M.3    Mukalov, I.O.4    Fedorovych, D.V.5    Sibirny, A.A.6
  • 41
    • 0032846825 scopus 로고    scopus 로고
    • Identification of an ARS element and development of a high efficiency transformation system for Pichia guilliermondii
    • Boretsky, Y., et al. 1999. Identification of an ARS element and development of a high efficiency transformation system for Pichia guilliermondii. Curr. Genet. 36:215-221.
    • (1999) Curr. Genet. , vol.36 , pp. 215-221
    • Boretsky, Y.1
  • 42
    • 79954424141 scopus 로고    scopus 로고
    • Identification of the genes affecting regulation of riboflavin synthesis in the flavinogenic yeast Pichia guilliermondii using insertion mutagenesis
    • Boretsky, Y. R., et al. 2011. Identification of the genes affecting regulation of riboflavin synthesis in the flavinogenic yeast Pichia guilliermondii using insertion mutagenesis. FEMS Yeast Res. 11:307-314.
    • (2011) FEMS Yeast Res. , vol.11 , pp. 307-314
    • Boretsky, Y.R.1
  • 43
    • 0036919327 scopus 로고    scopus 로고
    • Flavoenzymes that catalyse reactions with no net redox change
    • Bornemann, S. 2002. Flavoenzymes that catalyse reactions with no net redox change. Nat. Prod. Rep. 19:761-772.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 761-772
    • Bornemann, S.1
  • 44
    • 33748645974 scopus 로고    scopus 로고
    • Is the mycobacterial cell wall a hopeless drug target for latent tuberculosis?
    • Boshoff, H. I., and C. E. Barry III. 2006. Is the mycobacterial cell wall a hopeless drug target for latent tuberculosis? Drug Disc. Today Dis. Mech. 3:237-245.
    • (2006) Drug Disc. Today Dis. Mech. , vol.3 , pp. 237-245
    • Boshoff, H.I.1    Barry III, C.E.2
  • 45
    • 57649114083 scopus 로고    scopus 로고
    • Direct binding of GTP cyclohydrolase and tyrosine hydroxylase: Regulatory interactions between key enzymes in dopamine biosynthesis
    • Bowling, K. M., et al. 2008. Direct binding of GTP cyclohydrolase and tyrosine hydroxylase: regulatory interactions between key enzymes in dopamine biosynthesis. J. Biol. Chem. 283:31449-31459.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31449-31459
    • Bowling, K.M.1
  • 46
    • 0038825775 scopus 로고    scopus 로고
    • Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii
    • Brachat, S., et al. 2003. Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii. Genome Biol. 4:R45.
    • (2003) Genome Biol. , vol.4
    • Brachat, S.1
  • 47
    • 0032561180 scopus 로고    scopus 로고
    • Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase
    • Bracher, A., et al. 1998. Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase. J. Biol. Chem. 273:28132-28141.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28132-28141
    • Bracher, A.1
  • 48
    • 0034646571 scopus 로고    scopus 로고
    • Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus
    • Braden, B. C., C. A. Velikovsky, A. A. Cauerhff, I. Polikarpov, and F. A. Goldbaum. 2000. Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus. J. Mol. Biol. 297:1031-1036.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1031-1036
    • Braden, B.C.1    Velikovsky, C.A.2    Cauerhff, A.A.3    Polikarpov, I.4    Goldbaum, F.A.5
  • 49
    • 0012000445 scopus 로고
    • Study of the operon of riboflavin biosynthesis in Bacillus subtilis. V. Flavin mononucleotide and flavin adenine dinucleotide as effectors in the operon of riboflavin biosynthesis
    • In Russian
    • Bresler, S. E., E. A. Glazunov, T. P. Chernik, and D. A. Perumov. 1973. Study of the operon of riboflavin biosynthesis in Bacillus subtilis. V. Flavin mononucleotide and flavin adenine dinucleotide as effectors in the operon of riboflavin biosynthesis. Genetika 9:84-91. (In Russian.)
    • (1973) Genetika , vol.9 , pp. 84-91
    • Bresler, S.E.1    Glazunov, E.A.2    Chernik, T.P.3    Perumov, D.A.4
  • 50
    • 0018015364 scopus 로고
    • Riboflavin biosynthesis operon of Bacillus subtilis. XIV. Operator-constitutive mutants
    • Bresler, S. E., E. A. Glazunov, G. F. Gorinchuk, T. P. Chernik, and D. A. Perumov. 1978. Riboflavin biosynthesis operon of Bacillus subtilis. XIV. Operator-constitutive mutants. Genetika 14:1530-1538.
    • (1978) Genetika , vol.14 , pp. 1530-1538
    • Bresler, S.E.1    Glazunov, E.A.2    Gorinchuk, G.F.3    Chernik, T.P.4    Perumov, D.A.5
  • 51
    • 0040202254 scopus 로고
    • Study of the operon of riboflavin biosynthesis in Bacillus subtilis. IV. Regulation of the synthesis of riboflavin synthetase. Study of riboflavin transport through cell envelope
    • In Russian
    • Bresler, S. E., E. A. Glazunov, and D. A. Perumov. 1972. Study of the operon of riboflavin biosynthesis in Bacillus subtilis. IV. Regulation of the synthesis of riboflavin synthetase. Study of riboflavin transport through cell envelope. Genetika 8:109-117. (In Russian.)
    • (1972) Genetika , vol.8 , pp. 109-117
    • Bresler, S.E.1    Glazunov, E.A.2    Perumov, D.A.3
  • 52
    • 0017583309 scopus 로고
    • Riboflavin biosynthesis operon of Bacillus subtilis. XIII. Genetic and biochemical study of mutants with regard to intermediate stages of biosynthesis
    • In Russian
    • Bresler, S. E., E. A. Glazunov, D. A. Perumov, and T. P. Chernik. 1977. Riboflavin biosynthesis operon of Bacillus subtilis. XIII. Genetic and biochemical study of mutants with regard to intermediate stages of biosynthesis. Genetika 13:2006-2016. (In Russian.)
    • (1977) Genetika , vol.13 , pp. 2006-2016
    • Bresler, S.E.1    Glazunov, E.A.2    Perumov, D.A.3    Chernik, T.P.4
  • 53
    • 0008147504 scopus 로고
    • The mutant of Bacillus subtilis producing large amounts of riboflavin
    • In Russian
    • Bresler, S. E., V. L. Kalinin, A. S. Kriviskiy, and D. A. Perumov. 1969. The mutant of Bacillus subtilis producing large amounts of riboflavin. Genetika 5:133-138. (In Russian.)
    • (1969) Genetika , vol.5 , pp. 133-138
    • Bresler, S.E.1    Kalinin, V.L.2    Kriviskiy, A.S.3    Perumov, D.A.4
  • 54
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • Briggs, W. R., and J. M. Christie. 2002. Phototropins 1 and 2: versatile plant blue-light receptors. Trends Plant Sci. 7:204-210.
    • (2002) Trends Plant Sci. , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 55
    • 33745244792 scopus 로고    scopus 로고
    • Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase
    • Brizio, C., et al. 2006. Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase. Biochem. Biophys. Res. Commun. 344:1008-1016.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 1008-1016
    • Brizio, C.1
  • 56
    • 0022460313 scopus 로고
    • Regulation of flavin biosynthesis in the methylotrophie yeast Hansenula polymorpha
    • Brooke, A. G., L. Dijkhuizen, and W. Harder. 1986. Regulation of flavin biosynthesis in the methylotrophie yeast Hansenula polymorpha. Arch. Microbiol. 145:62-70.
    • (1986) Arch. Microbiol. , vol.145 , pp. 62-70
    • Brooke, A.G.1    Dijkhuizen, L.2    Harder, W.3
  • 57
    • 33947457572 scopus 로고
    • Paper chromatographic separation and determination of some water-soluble vitamins
    • Brown, J. A., and M. M. Marsh. 1952. Paper chromatographic separation and determination of some water-soluble vitamins. Anal. Chem. 24:1952-1956.
    • (1952) Anal. Chem. , vol.24 , pp. 1952-1956
    • Brown, J.A.1    Marsh, M.M.2
  • 58
    • 33646015669 scopus 로고    scopus 로고
    • The riboflavin transporter RibU in Lactococcus lactis: Molecular characterization of gene expression and the transport mechanism
    • Burgess, C. M., et al. 2006. The riboflavin transporter RibU in Lactococcus lactis: molecular characterization of gene expression and the transport mechanism. J. Bacteriol. 188:2752-2760.
    • (2006) J. Bacteriol. , vol.188 , pp. 2752-2760
    • Burgess, C.M.1
  • 59
    • 33749016265 scopus 로고    scopus 로고
    • A general method for selection of riboflavin-overproducing food grade micro-organisms
    • Burgess, C. M., E. J. Smid, G. Rutten, and D. van Sinderen. 2006. A general method for selection of riboflavin-overproducing food grade micro-organisms. Microb. Cell Fact. 5:24.
    • (2006) Microb. Cell Fact. , vol.5 , pp. 24
    • Burgess, C.M.1    Smid, E.J.2    Rutten, G.3    Van Sinderen, D.4
  • 61
    • 0018087061 scopus 로고
    • Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
    • Burrows, R. B., and G. M. Brown. 1978. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136:657-867.
    • (1978) J. Bacteriol. , vol.136 , pp. 657-867
    • Burrows, R.B.1    Brown, G.M.2
  • 62
    • 0034056390 scopus 로고    scopus 로고
    • LuxR- And acyl-homoserinelactone-controlled non-lux genes define a quorum-sensing regulon in Vibrio fischeri
    • Callahan, S. M., and P. V. Dunlap. 2000. LuxR- and acyl- homoserinelactone-controlled non-lux genes define a quorum-sensing regulon in Vibrio fischeri. J. Bacteriol. 182:2811-2822.
    • (2000) J. Bacteriol. , vol.182 , pp. 2811-2822
    • Callahan, S.M.1    Dunlap, P.V.2
  • 63
    • 39149114091 scopus 로고    scopus 로고
    • Controlled inactivation of recombinant viruses with vitamin B2
    • Callahan, S. M., et al. 2008. Controlled inactivation of recombinant viruses with vitamin B2. J. Virol. Methods 148:132-145.
    • (2008) J. Virol. Methods , vol.148 , pp. 132-145
    • Callahan, S.M.1
  • 67
    • 0013785270 scopus 로고
    • Flavin coenzymes, flavinogenesis and reproduction in Ashbya gossypii
    • Cerletti, P., R. Strom, M. G. Giordano, D. Barra, and S. Giovenco. 1965. Flavin coenzymes, flavinogenesis and reproduction in Ashbya gossypii. J. Biochem. 57:773-786.
    • (1965) J. Biochem. , vol.57 , pp. 773-786
    • Cerletti, P.1    Strom, R.2    Giordano, M.G.3    Barra, D.4    Giovenco, S.5
  • 68
    • 33745159681 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: Structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii
    • Chatwell, L., et al. 2006. Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii. J. Mol. Biol. 359:1334-1351.
    • (2006) J. Mol. Biol. , vol.359 , pp. 1334-1351
    • Chatwell, L.1
  • 69
    • 33646365634 scopus 로고    scopus 로고
    • Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis
    • Chen, S. C., Y. C. Chang, C. H. Lin, and S. H. Liaw. 2006. Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis. J. Biol. Chem. 281:7605-7613.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7605-7613
    • Chen, S.C.1    Chang, Y.C.2    Lin, C.H.3    Liaw, S.H.4
  • 70
    • 33748752430 scopus 로고    scopus 로고
    • The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow
    • Cheng, V. W., E. Ma, Z. Zhao, R. A. Rothery, and J. H. Weiner. 2006. The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow. J. Biol. Chem. 281:27662-27668.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27662-27668
    • Cheng, V.W.1    Ma, E.2    Zhao, Z.3    Rothery, R.A.4    Weiner, J.H.5
  • 71
    • 0035853757 scopus 로고    scopus 로고
    • Blue light sensing in higher plants
    • Christie, J. M., and W. R. Briggs. 2001. Blue light sensing in higher plants. J. Biol. Chem. 276:11457-11460.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11457-11460
    • Christie, J.M.1    Briggs, W.R.2
  • 72
    • 0015295052 scopus 로고
    • Inhibition of the phosphoribosylformylglycineamidine synthetase of Ehrlich ascites tumor cells by glutamine analogues
    • Chu, S. Y., and J. F. Henderson. 1972. Inhibition of the phosphoribosylformylglycineamidine synthetase of Ehrlich ascites tumor cells by glutamine analogues. Biochem. Pharmacol. 21:401-406.
    • (1972) Biochem. Pharmacol. , vol.21 , pp. 401-406
    • Chu, S.Y.1    Henderson, J.F.2
  • 73
    • 63049090478 scopus 로고    scopus 로고
    • Controlling the reactivity of chlorinated ethylenes with flavin mononucleotide hydroquinone
    • Ciptadjaya, C. G., W. Guo, J. M. Angeli, and S. O. Obare. 2009. Controlling the reactivity of chlorinated ethylenes with flavin mononucleotide hydroquinone. Environ. Sci. Technol. 43:1591-1597.
    • (2009) Environ. Sci. Technol. , vol.43 , pp. 1591-1597
    • Ciptadjaya, C.G.1    Guo, W.2    Angeli, J.M.3    Obare, S.O.4
  • 74
    • 0034925079 scopus 로고    scopus 로고
    • Macrolide resistance gene mreA of Streptococcus agalactiae encodes a flavokinase
    • Clarebout, G., C. Villers, and R. Leclercq. 2001. Macrolide resistance gene mreA of Streptococcus agalactiae encodes a flavokinase. Antimicrob. Agents Chemother. 45:2280-2286.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2280-2286
    • Clarebout, G.1    Villers, C.2    Leclercq, R.3
  • 75
    • 0024509968 scopus 로고
    • Discovery, production, and biological assay of an unusual flavenoid cofactor involved in lincomycin biosynthesis
    • Tokyo
    • Coats, J. H., G. P. Li, M. S. Kuo, and D. A. Yurek. 1989. Discovery, production, and biological assay of an unusual flavenoid cofactor involved in lincomycin biosynthesis. J. Antibiot. (Tokyo). 42:472-474.
    • (1989) J. Antibiot. , vol.42 , pp. 472-474
    • Coats, J.H.1    Li, G.P.2    Kuo, M.S.3    Yurek, D.A.4
  • 76
    • 44149111872 scopus 로고    scopus 로고
    • Riboswitch effectors as protein enzyme cofactors
    • Cochrane, J. C., and S. A. Strobel. 2008. Riboswitch effectors as protein enzyme cofactors. RNA 14:993-1002.
    • (2008) RNA , vol.14 , pp. 993-1002
    • Cochrane, J.C.1    Strobel, S.A.2
  • 77
    • 0040636712 scopus 로고
    • Riboflavin
    • J. Macklin (ed.), Marcel Dekker, New York, NY
    • Cooperman, J. M., and R. Lopez. 1991. Riboflavin, p. 283-310. In J. Macklin (ed.), Handbook of vitamins. Marcel Dekker, New York, NY.
    • (1991) Handbook of Vitamins , pp. 283-310
    • Cooperman, J.M.1    Lopez, R.2
  • 78
    • 73649141295 scopus 로고    scopus 로고
    • The Mtr respiratory pathway is essential for reducing flavins and electrodes in Shewanella oneidensis
    • Coursolle, D. D. B. Baron, D. R. Bond, and J. A. Gralnick. 2010. The Mtr respiratory pathway is essential for reducing flavins and electrodes in Shewanella oneidensis. J. Bacteriol. 192:467-474.
    • (2010) J. Bacteriol. , vol.192 , pp. 467-474
    • Coursolle, D.1    Baron, D.B.2    Bond, D.R.3    Gralnick, J.A.4
  • 79
    • 37349057886 scopus 로고    scopus 로고
    • Riboflavin biosynthesis is associated with assimilatory ferric reduction and iron acquisition by Campylobacter jejuni
    • Crossley, R. A., et al. 2007. Riboflavin biosynthesis is associated with assimilatory ferric reduction and iron acquisition by Campylobacter jejuni. Appl. Environ. Microbiol. 73:7819-7825.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7819-7825
    • Crossley, R.A.1
  • 80
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., E. Dassa, C. Orelle, and J. Chen. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72:317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 81
    • 0031428935 scopus 로고    scopus 로고
    • Determining covalent flavinylation
    • DOI 10.1016/S0076-6879(97)80133-4
    • Decker, K., and R. Brandsch. 1997. Determining covalent flavinylation. Methods Enzymol. 280:413-423. (Pubitemid 28182378)
    • (1997) Methods in Enzymology , vol.280 , pp. 413-423
    • Decker, K.1    Brandsch, R.2
  • 82
    • 34047180214 scopus 로고    scopus 로고
    • New frontiers in structural flavoenzymology
    • De Colibus, L., and A. Mattevi. 2006. New frontiers in structural flavoenzymology. Curr. Opin. Struct. Biol. 16:722-728.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 722-728
    • De Colibus, L.1    Mattevi, A.2
  • 83
    • 0001774745 scopus 로고
    • An unstable nuclear gene in Phycomyces
    • Delbrück, M., and T. Ootaki. 1979. An unstable nuclear gene in Phycomyces. Genetics 92:27-48.
    • (1979) Genetics , vol.92 , pp. 27-48
    • Delbrück, M.1    Ootaki, T.2
  • 84
    • 0015458831 scopus 로고
    • Riboflavin oversynthesis
    • Demain, A. L. 1972. Riboflavin oversynthesis. Annu. Rev. Microbiol. 26:369-388.
    • (1972) Annu. Rev. Microbiol. , vol.26 , pp. 369-388
    • Demain, A.L.1
  • 85
    • 36048992161 scopus 로고    scopus 로고
    • The business of biotechnology
    • Demain, A. L. 2007. The business of biotechnology. Ind. Biotechnol. 3:269-283.
    • (2007) Ind. Biotechnol. , vol.3 , pp. 269-283
    • Demain, A.L.1
  • 86
    • 0026165621 scopus 로고    scopus 로고
    • A serum-free, partly defined medium, PDM-805, for axenic cultivation of Entamoeba histolytica Schaudinn, 1903 and other Entamoeba
    • Diamond, L. S., and C. C. Cunnick. 2007. A serum-free, partly defined medium, PDM-805, for axenic cultivation of Entamoeba histolytica Schaudinn, 1903 and other Entamoeba. J. Eukaryot. Microbiol. 38:211-216.
    • (2007) J. Eukaryot. Microbiol. , vol.38 , pp. 211-216
    • Diamond, L.S.1    Cunnick, C.C.2
  • 88
    • 0015154264 scopus 로고
    • Yeast variants producing riboflavin and resistant to cobalt
    • In Russian
    • Dikanskaia, E. M. 1971. Yeast variants producing riboflavin and resistant to cobalt. Mikrobiologiia 40:1077-1083. (In Russian.)
    • (1971) Mikrobiologiia , vol.40 , pp. 1077-1083
    • Dikanskaia, E.M.1
  • 89
    • 0016547848 scopus 로고
    • Increased flavin synthesis in yeasts utilizing hydrocarbons
    • In Russian
    • Dikanskaia, E. M., and T. A. Gorobtsova. 1975. Increased flavin synthesis in yeasts utilizing hydrocarbons. Mikrobiologiia 44:784-790. (In Russian.)
    • (1975) Mikrobiologiia , vol.44 , pp. 784-790
    • Dikanskaia, E.M.1    Gorobtsova, T.A.2
  • 91
    • 3242702334 scopus 로고    scopus 로고
    • Cloning of structural genes involved in riboflavin synthesis of the yeast Candida famata
    • Dmytruk, K. V., et al. 2004. Cloning of structural genes involved in riboflavin synthesis of the yeast Candida famata. Ukr. Biokhim. Zhurn. 76:78-87.
    • (2004) Ukr. Biokhim. Zhurn. , vol.76 , pp. 78-87
    • Dmytruk, K.V.1
  • 92
    • 33747164466 scopus 로고    scopus 로고
    • Insertion mutagenesis of the yeast Candida famata (Debaryomyces hansenii) by random integration of linear DNA fragments
    • Dmytruk, K. V., A. Y. Voronovsky, and A. A. Sibirny. 2006. Insertion mutagenesis of the yeast Candida famata (Debaryomyces hansenii) by random integration of linear DNA fragments. Curr. Genet. 50:183-191.
    • (2006) Curr. Genet. , vol.50 , pp. 183-191
    • Dmytruk, K.V.1    Voronovsky, A.Y.2    Sibirny, A.A.3
  • 93
    • 78650629843 scopus 로고    scopus 로고
    • Metabolic engineering and classic selection of the yeast Candida famata (Candida flareri) for construction of the strains with enhanced riboflavin production
    • Dmytruk, K. V., V. Y. Yatsyshyn, D. V. Fedorovych, and A. A. Sibirny. 2011. Metabolic engineering and classic selection of the yeast Candida famata (Candida flareri) for construction of the strains with enhanced riboflavin production. Metab. Eng. 13:82-88.
    • (2011) Metab. Eng. , vol.13 , pp. 82-88
    • Dmytruk, K.V.1    Yatsyshyn, V.Y.2    Fedorovych, D.V.3    Sibirny, A.A.4
  • 94
    • 79958023464 scopus 로고
    • Purification of salts of riboflavin 5′-phosphate, in particular of monosodium riboflavin 5′-phosphate
    • January U.S. patent 4,987,229
    • Dobler, W., M. Eggersdorfer, and J. Paust. January 1991. Purification of salts of riboflavin 5′-phosphate, in particular of monosodium riboflavin 5′-phosphate. U.S. patent 4,987,229.
    • (1991)
    • Dobler, W.1    Eggersdorfer, M.2    Paust, J.3
  • 95
    • 0033861232 scopus 로고    scopus 로고
    • Riboflavin induces disease resistance in plants by activating a novel signal transduction pathway
    • Dong, H., and S. V. Beer. 2000. Riboflavin induces disease resistance in plants by activating a novel signal transduction pathway. Phytopathology 90:801-811.
    • (2000) Phytopathology , vol.90 , pp. 801-811
    • Dong, H.1    Beer, S.V.2
  • 96
    • 34147157826 scopus 로고    scopus 로고
    • Reporter proteins for in vivo fluorescence without oxygen
    • Drepper, T., et al. 2007. Reporter proteins for in vivo fluorescence without oxygen. Nat. Biotechnol. 25:443-445.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 443-445
    • Drepper, T.1
  • 97
    • 76849109846 scopus 로고    scopus 로고
    • Overexpression of glucose-6-phosphate dehydrogenase enhances riboflavin production in Bacillus subtilis
    • Duan, Y. X., T. Chen, X. Chen, and X. M. Zhao. 2010. Overexpression of glucose-6-phosphate dehydrogenase enhances riboflavin production in Bacillus subtilis. Appl. Microbiol. Biotechnol. 85:1907-1914.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1907-1914
    • Duan, Y.X.1    Chen, T.2    Chen, X.3    Zhao, X.M.4
  • 99
    • 0030956640 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: An unusual riboflavin synthase of Methanobacterium thermoautotrophicum
    • Eberhardt, S., S. Korn, F. Lottspeich, and A. Bacher. 1997. Biosynthesis of riboflavin: an unusual riboflavin synthase of Methanobacterium thermoautotrophicum. J. Bacteriol. 179:2938-2943. (Pubitemid 27194442)
    • (1997) Journal of Bacteriology , vol.179 , Issue.9 , pp. 2938-2943
    • Eberhardt, S.1    Korn, S.2    Lottspeich, F.3    Bacher, A.4
  • 100
    • 3843086171 scopus 로고    scopus 로고
    • Potential anti-infective targets in pathogenic yeasts: Structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans
    • Echt, S., et al. 2004. Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans. J. Mol. Biol. 341:1085-1096.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1085-1096
    • Echt, S.1
  • 101
    • 36248950938 scopus 로고    scopus 로고
    • General properties of flavins
    • E. Silva and A. M. Edwards (ed.), Flavins: photochemistry and photobiology. RSC, Cambridge, United Kingdom
    • Edwards, A. M. 2006. General properties of flavins, p. 1-11. In E. Silva and A. M. Edwards (ed.), Comprehensive series in photochemical and photobiological sciences, vol. 6. Flavins: photochemistry and photobiology. RSC, Cambridge, United Kingdom.
    • (2006) Comprehensive Series in Photochemical and Photobiological Sciences , vol.6 , pp. 1-11
    • Edwards, A.M.1
  • 102
    • 0032493472 scopus 로고    scopus 로고
    • Proposed steadystate kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli
    • Efimov, I., V. Kuusk, X. Zhang, and W. S. McIntire. 1998. Proposed steadystate kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli. Biochemistry 37:9716-9723.
    • (1998) Biochemistry , vol.37 , pp. 9716-9723
    • Efimov, I.1    Kuusk, V.2    Zhang, X.3    McIntire, W.S.4
  • 103
    • 0017389062 scopus 로고
    • Induction of FMN adenylyltransferase in the methanol utilizing yeast Candida boidinii
    • Eggeling, L., H. Sahm, and F. Wagner. 1977. Induction of FMN adenylyltransferase in the methanol utilizing yeast Candida boidinii. FEMS Microbiol. Lett. 1:205-211.
    • (1977) FEMS Microbiol. Lett. , vol.1 , pp. 205-211
    • Eggeling, L.1    Sahm, H.2    Wagner, F.3
  • 104
    • 0022764110 scopus 로고
    • Photoreactivating enzyme from Streptomyces griseus. VI. Action spectrum and kinetics of photoreactivation
    • Eker, A. P., J. K. Hessels, and R. H. Dekker. 1986. Photoreactivating enzyme from Streptomyces griseus. VI. Action spectrum and kinetics of photoreactivation. Photochem. Photobiol. 44:197-205.
    • (1986) Photochem. Photobiol. , vol.44 , pp. 197-205
    • Eker, A.P.1    Hessels, J.K.2    Dekker, R.H.3
  • 105
    • 0025272139 scopus 로고
    • DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans
    • Eker, A. P. M., P. Kooiman, J. K. Hessels, and A. Yasui. 1990. DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265:8009-8015.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8009-8015
    • Eker, A.P.M.1    Kooiman, P.2    Hessels, J.K.3    Yasui, A.4
  • 106
    • 62449152157 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: Direct DNA damage reversal: Elegant solutions for nasty problems
    • Eker, A. P., C. Quayle, I. Chaves, and G. T. van der Horst. 2009. DNA repair in mammalian cells: direct DNA damage reversal: elegant solutions for nasty problems. Cell Mol. Life Sci. 66:968-980.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 968-980
    • Eker, A.P.1    Quayle, C.2    Chaves, I.3    Van Der Horst, G.T.4
  • 107
    • 0005083408 scopus 로고
    • Effect of cobalt and iron on riboflavin by Candida guilliermondii
    • Enary, T. M. 1955. Effect of cobalt and iron on riboflavin by Candida guilliermondii. Acta Chem. Scand. 9:1726-1729.
    • (1955) Acta Chem. Scand. , vol.9 , pp. 1726-1729
    • Enary, T.M.1
  • 108
    • 0026633013 scopus 로고
    • 6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae
    • Exinger, F., and F. Lacroute. 1992. 6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae. Curr. Genet. 22:9-11.
    • (1992) Curr. Genet. , vol.22 , pp. 9-11
    • Exinger, F.1    Lacroute, F.2
  • 109
    • 0034668291 scopus 로고    scopus 로고
    • Structural and functional analysis of the riboflavin synthesis genes encoding GTP cyclohydrolase II (ribA), DHBP synthase (ribBA), riboflavin synthase (ribC), and riboflavin deaminase/reductase (ribD) from Helicobacter pylori strain P1
    • Fassbinder, F., M. Kist, and S. Bereswill. 2000. Structural and functional analysis of the riboflavin synthesis genes encoding GTP cyclohydrolase II (ribA), DHBP synthase (ribBA), riboflavin synthase (ribC), and riboflavin deaminase/reductase (ribD) from Helicobacter pylori strain P1. FEMS Microbiol. Lett. 191:191-197.
    • (2000) FEMS Microbiol. Lett. , vol.191 , pp. 191-197
    • Fassbinder, F.1    Kist, M.2    Bereswill, S.3
  • 110
    • 0005030653 scopus 로고    scopus 로고
    • Accumulation and redox transformations of iron on the yeast Pichia guilliermondii and its flavinogenic mutants
    • In Rusian
    • Fedorovich, D. V., I. V. Kityk, V. I. Dzhala, O. V. Protchenko, and G. M. Shavlovskii. 1997. Accumulation and redox transformations of iron on the yeast Pichia guilliermondii and its flavinogenic mutants. Mikrobiologiia 66:60-64. (In Rusian.)
    • (1997) Mikrobiologiia , vol.66 , pp. 60-64
    • Fedorovich, D.V.1    Kityk, I.V.2    Dzhala, V.I.3    Protchenko, O.V.4    Shavlovskii, G.M.5
  • 111
    • 0033493506 scopus 로고    scopus 로고
    • Iron uptake by the yeast Pichia guilliermondii. Flavinogenesis and reductive iron assimilation are co-regulated processes
    • Fedorovich, D., O. Protchenko, and E. Lesuisse. 1999. Iron uptake by the yeast Pichia guilliermondii. Flavinogenesis and reductive iron assimilation are co-regulated processes. Biometals 12:295-300.
    • (1999) Biometals , vol.12 , pp. 295-300
    • Fedorovich, D.1    Protchenko, O.2    Lesuisse, E.3
  • 112
    • 0035028540 scopus 로고    scopus 로고
    • Hexavalent chromium stimulation of riboflavin synthesis in flavinogenic yeast
    • DOI 10.1023/A:1016643307690
    • Fedorovych, D., H. Kszeminska, L. Babjak, P. Kaszycki, and H. Koloczek. 2001. Hexavalent chromium stimulation of riboflavin synthesis in flavinogenic yeast. Biometals 14:23-31. (Pubitemid 32391795)
    • (2001) BioMetals , vol.14 , Issue.1 , pp. 23-31
    • Fedorovych, D.1    Kszeminska, H.2    Babjak, L.3    Kaszycki, P.4    Koloczek, H.5
  • 113
    • 21244445102 scopus 로고    scopus 로고
    • Biosynthesis of flavocoenzymes
    • Fischer, M., and A. Bacher. 2005. Biosynthesis of flavocoenzymes. Nat. Prod. Rep. 22:324-350.
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 324-350
    • Fischer, M.1    Bacher, A.2
  • 115
    • 44549086610 scopus 로고    scopus 로고
    • 2: Structure and mechanism of riboflavin synthase
    • 2: structure and mechanism of riboflavin synthase. Arch. Biochem. Biophys. 474:252-265.
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 252-265
    • Fischer, M.1    Bacher, A.2
  • 116
    • 79958060348 scopus 로고    scopus 로고
    • Riboflavin biosynthesis
    • L. Mander, and H. W. Liu (ed.), Cofactors. Elsevier, Philadelphia, PA
    • Fischer, M., and A. Bacher. 2010. Riboflavin biosynthesis, p. 3-36. In L. Mander, and H. W. Liu (ed.), Comprehensive natural products. II. Chemistry and biology, vol. 7. Cofactors. Elsevier, Philadelphia, PA.
    • (2010) Comprehensive Natural Products. II. Chemistry and Biology , vol.7 , pp. 3-36
    • Fischer, M.1    Bacher, A.2
  • 117
    • 0036161814 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe
    • Fischer, M., et al. 2002. Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. Eur. J. Biochem. 269:519-526.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 519-526
    • Fischer, M.1
  • 118
    • 23844514072 scopus 로고    scopus 로고
    • Evolution of vitamin B2 biosynthesis: Riboflavin synthase of Arabidopsis thaliana and its inhibition by riboflavin
    • Fischer, M., et al. 2005. Evolution of vitamin B2 biosynthesis: riboflavin synthase of Arabidopsis thaliana and its inhibition by riboflavin. Biol. Chem. 386:417-428.
    • (2005) Biol. Chem. , vol.386 , pp. 417-428
    • Fischer, M.1
  • 119
    • 0037459044 scopus 로고    scopus 로고
    • Enzyme catalysis via control of activation entropy: Site-directed mutagenesis of 6,7-dimethyl-8-ribityllumazine synthase
    • Fischer, M., et al. 2003. Enzyme catalysis via control of activation entropy: site-directed mutagenesis of 6,7-dimethyl-8-ribityllumazine synthase. J. Mol. Biol. 326:783-793.
    • (2003) J. Mol. Biol. , vol.326 , pp. 783-793
    • Fischer, M.1
  • 120
    • 4344648767 scopus 로고    scopus 로고
    • 2 biosynthesis: Structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin
    • 2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin. J. Biol. Chem. 279:36299-36308.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36299-36308
    • Fischer, M.1
  • 121
    • 0036829021 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin in archaea: Studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii
    • Fischer, M., et al. 2002. Biosynthesis of riboflavin in archaea: studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii. J. Biol. Chem. 277:41410-41416.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41410-41416
    • Fischer, M.1
  • 122
    • 4644264487 scopus 로고    scopus 로고
    • Evolution of vitamin B2 biosynthesis. A novel class of riboflavin synthase in Archaea
    • Fischer, M., et al. 2004. Evolution of vitamin B2 biosynthesis. A novel class of riboflavin synthase in Archaea. J. Mol. Biol. 343:267-278.
    • (2004) J. Mol. Biol. , vol.343 , pp. 267-278
    • Fischer, M.1
  • 124
    • 0016789502 scopus 로고
    • Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli
    • Foor, F., and G. M. Brown. 1975. Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J. Biol. Chem. 250:3545-3551.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3545-3551
    • Foor, F.1    Brown, G.M.2
  • 125
    • 0018814647 scopus 로고
    • GTP cyclohydrolase II from Escherichia coli
    • Foor, F., and G. M. Brown. 1980. GTP cyclohydrolase II from Escherichia coli. Methods Enzymol. 66:303-307.
    • (1980) Methods Enzymol. , vol.66 , pp. 303-307
    • Foor, F.1    Brown, G.M.2
  • 126
    • 0345714785 scopus 로고    scopus 로고
    • Current perspectives in cellular uptake and trafficking of riboflavin
    • Foraker, A. B., C. M. Khantwal, and P. W. Swaan. 2003. Current perspectives in cellular uptake and trafficking of riboflavin. Adv. Drug Deliv. Rev. 55:1467-1483.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1467-1483
    • Foraker, A.B.1    Khantwal, C.M.2    Swaan, P.W.3
  • 127
    • 45549109689 scopus 로고    scopus 로고
    • Molecular insights into the biosynthesis of the F420 coenzyme
    • Forouhar, F., et al. 2008. Molecular insights into the biosynthesis of the F420 coenzyme. J. Biol. Chem. 283:11832-11840.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11832-11840
    • Forouhar, F.1
  • 129
    • 0037940408 scopus 로고    scopus 로고
    • Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii
    • Förster, C., M. A. Santos, S. Ruffert, R. Krämer, and J. L. Revuelta. 1999. Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii. J. Biol. Chem. 274:9442-9448.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9442-9448
    • Förster, C.1    Santos, M.A.2    Ruffert, S.3    Krämer, R.4    Revuelta, J.L.5
  • 131
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M. V., and A. Mattevi. 2000. Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 25:126-132.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.V.1    Mattevi, A.2
  • 132
    • 0033544926 scopus 로고    scopus 로고
    • Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase
    • Fraaije, M. W., R. H. van den Heuvel, W. J. van Berkel, and A. Mattevi. 1999. Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase. J. Biol. Chem. 274:35514-35520.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35514-35520
    • Fraaije, M.W.1    Van Den Heuvel, R.H.2    Van Berkel, W.J.3    Mattevi, A.4
  • 133
    • 0019991801 scopus 로고
    • Nutritional requirements of Corynebacterium pyogenes
    • Fraga, A. A., and C. A. Reddy. 1982. Nutritional requirements of Corynebacterium pyogenes. J. Clin. Microbiol. 16:334-340.
    • (1982) J. Clin. Microbiol. , vol.16 , pp. 334-340
    • Fraga, A.A.1    Reddy, C.A.2
  • 134
    • 54949103490 scopus 로고    scopus 로고
    • Structural analysis of FAD synthetase from Corynebacterium ammoniagenes
    • Frago, S., M. Martínez-Júlvez, A. Serrano, and M. Medina. 2008. Structural analysis of FAD synthetase from Corynebacterium ammoniagenes. BMC Microbiol. 8:160.
    • (2008) BMC Microbiol. , vol.8 , pp. 160
    • Frago, S.1    Martínez-Júlvez, M.2    Serrano, A.3    Medina, M.4
  • 135
    • 65449140334 scopus 로고    scopus 로고
    • The puzzle of ligand binding to Corynebacterium ammoniagenes FAD synthetase
    • Frago, S., A. Velázquez-Campoy, and M. Medina. 2009. The puzzle of ligand binding to Corynebacterium ammoniagenes FAD synthetase. J. Biol. Chem. 284:6610-6619.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6610-6619
    • Frago, S.1    Velázquez-Campoy, A.2    Medina, M.3
  • 136
    • 0037008528 scopus 로고    scopus 로고
    • White Collar-1, a circadian blue light photoreceptor, binding to the frequency promoter
    • Froehlich, A. C., Y. Liu, J. J. Loros, and J. C. Dunlap. 2002. White Collar-1, a circadian blue light photoreceptor, binding to the frequency promoter. Science 297:815-819.
    • (2002) Science , vol.297 , pp. 815-819
    • Froehlich, A.C.1    Liu, Y.2    Loros, J.J.3    Dunlap, J.C.4
  • 137
    • 0031171045 scopus 로고    scopus 로고
    • Enzymatic production of pyrimidine nucleotides using Corynebacterium ammoniagenes cells and recombinant Escherichia coli cells: Enzymatic production of CDP-choline from orotic acid and choline chloride (part I)
    • Fujio, T., and A. Maruyama. 1997. Enzymatic production of pyrimidine nucleotides using Corynebacterium ammoniagenes cells and recombinant Escherichia coli cells: enzymatic production of CDP-choline from orotic acid and choline chloride (part I). Biosci. Biotechnol. Biochem. 61:956-959.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 956-959
    • Fujio, T.1    Maruyama, A.2
  • 138
    • 0028799175 scopus 로고
    • The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8- ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein
    • García-Ramírez, J. J., M. A. Santos, and J. L. Revuelta. 1995. The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8- ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein. J. Biol. Chem. 270:23801-23807.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23801-23807
    • García-Ramírez, J.J.1    Santos, M.A.2    Revuelta, J.L.3
  • 139
    • 0033230755 scopus 로고    scopus 로고
    • A conserved RNA structure element involved in the regulation of bacterial riboflavin synthesis genes
    • Gelfand, M. S., A. A. Mironov, J. Jomantas, Y. I. Kozlov, and D. A. Perumov. 1999. A conserved RNA structure element involved in the regulation of bacterial riboflavin synthesis genes. Trends Genet. 15:439-442.
    • (1999) Trends Genet. , vol.15 , pp. 439-442
    • Gelfand, M.S.1    Mironov, A.A.2    Jomantas, J.3    Kozlov, Y.I.4    Perumov, D.A.5
  • 140
    • 0036315369 scopus 로고    scopus 로고
    • The structural basis of riboflavin binding to Schizosaccharomyces pombe 6,7-dimethyl-8-ribityllumazine synthase
    • Gerhardt, S., et al. 2002. The structural basis of riboflavin binding to Schizosaccharomyces pombe 6,7-dimethyl-8-ribityllumazine synthase. J. Mol. Biol. 318:1317-1329.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1317-1329
    • Gerhardt, S.1
  • 143
    • 0017280141 scopus 로고
    • Identification and properties of 8-hydroxyflavin- adenine dinucleotide in electron-transferring flavoprotein from Peptostreptococcus elsdenii
    • Ghisla, S., and S. G. Mayhew. 1976. Identification and properties of 8-hydroxyflavin- adenine dinucleotide in electron-transferring flavoprotein from Peptostreptococcus elsdenii. Eur. J. Biochem. 63:373-390.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 373-390
    • Ghisla, S.1    Mayhew, S.G.2
  • 144
    • 57649227455 scopus 로고    scopus 로고
    • The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status
    • Giancaspero, T. A., V. Locato, M. C. de Pinto, L. De Gara, and M. Barile. 2009. The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status. FEBS J. 276:219-231.
    • (2009) FEBS J. , vol.276 , pp. 219-231
    • Giancaspero, T.A.1    Locato, V.2    De Pinto, M.C.3    De Gara, L.4    Barile, M.5
  • 145
    • 40349094993 scopus 로고    scopus 로고
    • Succinate dehydrogenase flavoprotein subunit expression in Saccharomyces cerevisiae - Involvement of the mitochondrial FAD transporter, Flx1p
    • DOI 10.1111/j.1742-4658.2008.06270.x
    • Giancaspero, T. A., R. Wait, E. Boles, and M. Barile. 2008. Succinate dehydrogenase flavoprotein subunit expression in Saccharomyces cerevisiae - involvement of the mitochondrial FAD transporter, Flx1p. FEBS J. 275:1103-1117. (Pubitemid 351342207)
    • (2008) FEBS Journal , vol.275 , Issue.6 , pp. 1103-1117
    • Giancaspero, T.A.1    Wait, R.2    Boles, E.3    Barile, M.4
  • 146
    • 33644786204 scopus 로고
    • Occurrence of flavokinase activity in plants
    • Giri, K. V., P. W. Krishnaswamy, and N. A. Rao. 1957. Occurrence of flavokinase activity in plants. Nature 179:1134-1135.
    • (1957) Nature , vol.179 , pp. 1134-1135
    • Giri, K.V.1    Krishnaswamy, P.W.2    Rao, N.A.3
  • 147
    • 67650915115 scopus 로고    scopus 로고
    • The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes
    • Glas, A. F., et al. 2009. The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes. Proc. Natl. Acad. Sci. U. S. A. 106:11540-11545.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11540-11545
    • Glas, A.F.1
  • 148
    • 0032566485 scopus 로고    scopus 로고
    • Chromatographic determination of flavin derivatives in baker's yeast
    • Gliszczynska, A., and A. Koziolowa. 1998. Chromatographic determination of flavin derivatives in baker's yeast. J. Chromatogr. A 822:59-66.
    • (1998) J. Chromatogr. A , vol.822 , pp. 59-66
    • Gliszczynska, A.1    Koziolowa, A.2
  • 149
    • 0036804709 scopus 로고    scopus 로고
    • BLUF: A novel FAD-binding domain involved in sensory transduction in microorganisms
    • Gomelsky, M., and G. Klug. 2002. BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem. Sci. 27:497-500.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 150
    • 77749273577 scopus 로고    scopus 로고
    • Flavin adenine dinucleotide rescues the phenotype of frataxin deficiency
    • Gonzalez-Cabo, P., S. Ros, and F. Palau. 2010. Flavin adenine dinucleotide rescues the phenotype of frataxin deficiency. PLoS One 5:e8872.
    • (2010) PLoS One , vol.5
    • Gonzalez-Cabo, P.1    Ros, S.2    Palau, F.3
  • 151
    • 26844526809 scopus 로고
    • Studies on the biosynthesis of riboflavin. 5. General factors controlling flavinogenesis in the yeast Candida flareri
    • Goodwin, T. W., and D. McEvoy. 1959. Studies on the biosynthesis of riboflavin. 5. General factors controlling flavinogenesis in the yeast Candida flareri. Biochem. J. 71:742-748.
    • (1959) Biochem. J. , vol.71 , pp. 742-748
    • Goodwin, T.W.1    McEvoy, D.2
  • 152
    • 0036005602 scopus 로고    scopus 로고
    • Elucidation of methanogenic coenzyme biosyntheses: From spectroscopy to genomics
    • Graham, D. E., and R. H. White. 2002. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19:133-147.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 133-147
    • Graham, D.E.1    White, R.H.2
  • 154
    • 0036203061 scopus 로고    scopus 로고
    • 420 biosynthesis in Archaea proceeds by the eukaryotic route to riboflavin
    • 420 biosynthesis in Archaea proceeds by the eukaryotic route to riboflavin. J. Bacteriol. 184:1952-1957.
    • (2002) J. Bacteriol. , vol.184 , pp. 1952-1957
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 156
    • 39749093132 scopus 로고    scopus 로고
    • The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
    • DOI 10.1128/JB.01586-07
    • Grill, S., S. Busenbender, M. Pfeiffer, U. Köhler, and M. Mack. 2008. The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin. J. Bacteriol. 190:1546-1553. (Pubitemid 351304008)
    • (2008) Journal of Bacteriology , vol.190 , Issue.5 , pp. 1546-1553
    • Grill, S.1    Busenbender, S.2    Pfeiffer, M.3    Kohler, U.4    Mack, M.5
  • 157
    • 34548667967 scopus 로고    scopus 로고
    • Identification and characterization of two Streptomyces davawensis riboflavin biosynthesis gene clusters
    • Grill, S., et al. 2007. Identification and characterization of two Streptomyces davawensis riboflavin biosynthesis gene clusters. Arch. Microbiol. 188:377-387.
    • (2007) Arch. Microbiol. , vol.188 , pp. 377-387
    • Grill, S.1
  • 159
    • 33644939828 scopus 로고    scopus 로고
    • Dodecins: A family of lumichrome binding proteins
    • Grininger, M., K. Zeith, and D. Oesterhelt. 2006. Dodecins: a family of lumichrome binding proteins. J. Mol. Biol. 357:842-857.
    • (2006) J. Mol. Biol. , vol.357 , pp. 842-857
    • Grininger, M.1    Zeith, K.2    Oesterhelt, D.3
  • 160
    • 40149100332 scopus 로고    scopus 로고
    • Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F420 biosynthesis
    • Grochowski, L. L., H. Xu, and R. H. White. 2008. Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F420 biosynthesis. Biochemistry 47:3033-3037.
    • (2008) Biochemistry , vol.47 , pp. 3033-3037
    • Grochowski, L.L.1    Xu, H.2    White, R.H.3
  • 161
    • 66049090396 scopus 로고    scopus 로고
    • An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5- deazariboflavin
    • Grochowski, L. L., H. Xu, and R. H. White. 2009. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48:4181-4188.
    • (2009) Biochemistry , vol.48 , pp. 4181-4188
    • Grochowski, L.L.1    Xu, H.2    White, R.H.3
  • 162
    • 0032518643 scopus 로고    scopus 로고
    • Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene
    • Groom, K. R., H. C. Heyman, M. C. Steffen, L. Hawkins, and N. C. Martin. 1998. Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene. Yeast 14:77-87.
    • (1998) Yeast , vol.14 , pp. 77-87
    • Groom, K.R.1    Heyman, H.C.2    Steffen, M.C.3    Hawkins, L.4    Martin, N.C.5
  • 163
    • 2442650455 scopus 로고
    • Sur l'existence dans l'Eremothecium ashbyii d'un pigment jaune se rapportant au groupe des flavines
    • Guilliermond, A., M. Fontaine, and A. Raffy. 1935. Sur l'existence dans l'Eremothecium ashbyii d'un pigment jaune se rapportant au groupe des flavines. C. R. Hebd. Seances Acad. Sci. 201:1077-1080.
    • (1935) C. R. Hebd. Seances Acad. Sci. , vol.201 , pp. 1077-1080
    • Guilliermond, A.1    Fontaine, M.2    Raffy, A.3
  • 164
    • 0031217883 scopus 로고    scopus 로고
    • Primary structure and functional activity of the Bacillus subtilis ribC gene
    • Moscow
    • Gusarov, I. I., et al. 1997. Primary structure and functional activity of the Bacillus subtilis ribC gene. Mol. Biol. (Moscow) 31:820-825.
    • (1997) Mol. Biol. , vol.31 , pp. 820-825
    • Gusarov, I.I.1
  • 165
    • 0028798483 scopus 로고
    • Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production
    • Hagihara, T., T. Fujio, and K. Aisaka. 1995. Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production. Appl. Microbiol. Biotechnol. 42:724-729.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 724-729
    • Hagihara, T.1    Fujio, T.2    Aisaka, K.3
  • 166
    • 0014010572 scopus 로고
    • Riboflavin synthetase from yeast. Properties of complexes of the enzyme with lumazine derivatives and riboflavin
    • Harvey, R. A., and G. W. Plaut. 1966. Riboflavin synthetase from yeast. Properties of complexes of the enzyme with lumazine derivatives and riboflavin. J. Biol. Chem. 241:2120-2136.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2120-2136
    • Harvey, R.A.1    Plaut, G.W.2
  • 167
    • 0002942498 scopus 로고    scopus 로고
    • Chloroplast movement: From phenomenology to molecular biology
    • Haupt, W. 1999. Chloroplast movement: from phenomenology to molecular biology. Prog. Bot. 60:3-35.
    • (1999) Prog. Bot. , vol.60 , pp. 3-35
    • Haupt, W.1
  • 168
    • 33847315165 scopus 로고    scopus 로고
    • Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module
    • Hebbeln, P., D. A. Rodionov, A. Alfandega, and T. Eitinger. 2007. Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module. Proc. Natl. Acad. Sci. U. S. A. 104:2909-2914.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2909-2914
    • Hebbeln, P.1    Rodionov, D.A.2    Alfandega, A.3    Eitinger, T.4
  • 169
    • 4244071443 scopus 로고
    • Efficient riboflavin production with yeast
    • July U.S. patent 5,231,007
    • Heefner, D. L. A. Boyts, L. Burdzinski, and M. Yarus. July 1993. Efficient riboflavin production with yeast. U.S. patent 5,231,007.
    • (1993)
    • Heefner, D.L.1    Boyts, A.2    Burdzinski, L.3    Yarus, M.4
  • 170
    • 0003716457 scopus 로고
    • Riboflavin producing strains of microorganisms, method for selecting, and method for fermentation
    • December Patent WO 88/09822
    • Heefner, D., et al. December 1988. Riboflavin producing strains of microorganisms, method for selecting, and method for fermentation. Patent WO 88/09822.
    • (1988)
    • Heefner, D.1
  • 171
    • 0008096647 scopus 로고
    • Method for producing riboflavin with Candida famata
    • November U.S. patent 5,164,303
    • Heefner, D. L., C. A. Weaver, M. J. Yarus, and L. A. Burdzinski. November 1992. Method for producing riboflavin with Candida famata. U.S. patent 5,164,303.
    • (1992)
    • Heefner, D.L.1    Weaver, C.A.2    Yarus, M.J.3    Burdzinski, L.A.4
  • 172
    • 0017666039 scopus 로고
    • Flavin and 5-deazaflavin: A chemical evaluation of 'modified' flavoproteins with respect to the mechanisms of redox biocatalysis
    • Hemmerich, P., V. Massey, and H. Fenner. 1977. Flavin and 5-deazaflavin: a chemical evaluation of 'modified' flavoproteins with respect to the mechanisms of redox biocatalysis. FEBS Lett. 84:5-21.
    • (1977) FEBS Lett. , vol.84 , pp. 5-21
    • Hemmerich, P.1    Massey, V.2    Fenner, H.3
  • 173
    • 0018427259 scopus 로고
    • Coupling of energy to folate transport in Lactobacillus casei
    • Henderson, G. B., E. M. Zevely, and G. M. Huennekens. 1979. Coupling of energy to folate transport in Lactobacillus casei. J. Bacteriol. 139:552-559.
    • (1979) J. Bacteriol. , vol.139 , pp. 552-559
    • Henderson, G.B.1    Zevely, E.M.2    Huennekens, G.M.3
  • 174
    • 77953810360 scopus 로고    scopus 로고
    • Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes
    • Herguedas, B., M. Martínez-Júlvez, S. Frago, M. Medina, and J. A. Hermoso. 2010. Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes. J. Mol. Biol. 400:218-230.
    • (2010) J. Mol. Biol. , vol.400 , pp. 218-230
    • Herguedas, B.1    Martínez-Júlvez, M.2    Frago, S.3    Medina, M.4    Hermoso, J.A.5
  • 175
    • 0034615904 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin in plants. The ribA gene of Arabidopsis thaliana specifies a bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase
    • Herz, S., S. Eberhardt, and A. Bacher. 2000. Biosynthesis of riboflavin in plants. The ribA gene of Arabidopsis thaliana specifies a bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase. Phytochemistry 53:723-731.
    • (2000) Phytochemistry , vol.53 , pp. 723-731
    • Herz, S.1    Eberhardt, S.2    Bacher, A.3
  • 176
    • 52549117825 scopus 로고
    • The inactivation of iron by 2,2′-bipyrimidine and its effect on riboflavin synthesis by Clostridium acetobutylicum
    • Hickey, R. J. 1945. The inactivation of iron by 2,2′-bipyrimidine and its effect on riboflavin synthesis by Clostridium acetobutylicum. Arch. Biochem. 8:439-447.
    • (1945) Arch. Biochem. , vol.8 , pp. 439-447
    • Hickey, R.J.1
  • 177
    • 42049123458 scopus 로고    scopus 로고
    • Root tip-dependent, active riboflavin secretion by Hyoscyamus albus hairy roots under iron deficiency
    • Higa, A., E. Miyamoto, L. ur Rahman, and Y. Kitamura. 2008. Root tip-dependent, active riboflavin secretion by Hyoscyamus albus hairy roots under iron deficiency. Plant Physiol. Biochem. 46:452-460.
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 452-460
    • Higa, A.1    Miyamoto, E.2    Ur Rahman, L.3    Kitamura, Y.4
  • 178
    • 34547462532 scopus 로고    scopus 로고
    • RibR, a possible regulator of the Bacillus subtilis riboflavin biosynthetic operon, in vivo interacts with the 5′-untranslated leader of rib mRNA
    • Higashitsuji, Y., A. Angerer, S. Berghaus, B. Hobl, and M. Mack. 2007. RibR, a possible regulator of the Bacillus subtilis riboflavin biosynthetic operon, in vivo interacts with the 5′-untranslated leader of rib mRNA. FEMS Microbiol. Lett. 274:48-54.
    • (2007) FEMS Microbiol. Lett. , vol.274 , pp. 48-54
    • Higashitsuji, Y.1    Angerer, A.2    Berghaus, S.3    Hobl, B.4    Mack, M.5
  • 179
    • 79958038701 scopus 로고    scopus 로고
    • Biotechnology of riboflavin production
    • L. Mander, and H. W. Liu (ed.), Cofactors. Elsevier, Philadelphia, PA
    • Hohmann, H. P., and K. P. Stahmann. 2010. Biotechnology of riboflavin production, p. 115-139. In L. Mander, and H. W. Liu (ed.), Comprehensive natural products. II. Chemistry and biology, vol. 7. Cofactors. Elsevier, Philadelphia, PA.
    • (2010) Comprehensive Natural Products. II. Chemistry and Biology , vol.7 , pp. 115-139
    • Hohmann, H.P.1    Stahmann, K.P.2
  • 180
    • 0018802668 scopus 로고
    • Biosynthesis of riboflavin: Reductase and deaminase of Ashbya gossypii
    • Hollander, I., and G. M. Brown. 1979. Biosynthesis of riboflavin: reductase and deaminase of Ashbya gossypii. Biochem. Biophys. Res. Commun. 89:759-763.
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 759-763
    • Hollander, I.1    Brown, G.M.2
  • 181
    • 0345492925 scopus 로고
    • Riboflavine. XII. Requirements and factors influencing them
    • W. H. Sebrell and R. S. Harris (ed.), Academic Press, New York, NY
    • Horwitt, M. K. 1972. Riboflavine. XII. Requirements and factors influencing them, p. 73-88. In W. H. Sebrell and R. S. Harris (ed.), The vitamins, vol. 5. Academic Press, New York, NY.
    • (1972) The Vitamins , vol.5 , pp. 73-88
    • Horwitt, M.K.1
  • 182
    • 0030872578 scopus 로고    scopus 로고
    • D-Erythro-neopterin biosynthesis in the methanogenic archaea Methanococcus thermophila and Methanobacterium thermoautotrophicum deltaH
    • Howell, D. M., and R. H. White. 1997. D-Erythro-neopterin biosynthesis in the methanogenic archaea Methanococcus thermophila and Methanobacterium thermoautotrophicum deltaH. J. Bacteriol. 179:5165-5170.
    • (1997) J. Bacteriol. , vol.179 , pp. 5165-5170
    • Howell, D.M.1    White, R.H.2
  • 183
    • 0034978262 scopus 로고    scopus 로고
    • Riboflavin uptake in human trophoblast-derived BeWo cell monolayers: Cellular translocation and regulatory mechanisms
    • Huang, S. N., and P. W. Swaan. 2001. Riboflavin uptake in human trophoblast-derived BeWo cell monolayers: cellular translocation and regulatory mechanisms. J. Pharmacol. Exp. Ther. 298:264-271.
    • (2001) J. Pharmacol. Exp. Ther. , vol.298 , pp. 264-271
    • Huang, S.N.1    Swaan, P.W.2
  • 184
    • 69249212126 scopus 로고    scopus 로고
    • Thapsigargin and flavin adenine dinucleotide ex vivo treatment rescues trafficking-defective gp91phox in chronic granulomatous disease leukocytes
    • Huang, Y. F., S. Y. Liu, C. L. Yen, P. W. Yang, and C. C. Shieh. 2009. Thapsigargin and flavin adenine dinucleotide ex vivo treatment rescues trafficking-defective gp91phox in chronic granulomatous disease leukocytes. Free Radic. Biol. Med. 47:932-940.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 932-940
    • Huang, Y.F.1    Liu, S.Y.2    Yen, C.L.3    Yang, P.W.4    Shieh, C.C.5
  • 185
    • 65549115599 scopus 로고    scopus 로고
    • Structure and mechanism of a eukaryotic FMN adenylyltransferase
    • Huerta, C., D. Borek, M. Machius, N. V. Grishin, and H. Zhang. 2009. Structure and mechanism of a eukaryotic FMN adenylyltransferase. J. Mol. Biol. 389:388-400.
    • (2009) J. Mol. Biol. , vol.389 , pp. 388-400
    • Huerta, C.1    Borek, D.2    Machius, M.3    Grishin, N.V.4    Zhang, H.5
  • 186
    • 0033040385 scopus 로고    scopus 로고
    • GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase are rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production
    • Hümbelin, M., et al. 1999. GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase are rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production. J. Ind. Microbiol. Biotechnol. 22:1-7.
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.22 , pp. 1-7
    • Hümbelin, M.1
  • 187
    • 0033025596 scopus 로고    scopus 로고
    • Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma by capillary electrophoresis and laser-induced fluorescence detection
    • Hustad, S., P. M. Ueland, and J. Schneede. 1999. Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma by capillary electrophoresis and laser-induced fluorescence detection. Clin. Chem. 45:862-868.
    • (1999) Clin. Chem. , vol.45 , pp. 862-868
    • Hustad, S.1    Ueland, P.M.2    Schneede, J.3
  • 188
    • 59649087411 scopus 로고    scopus 로고
    • Riboflavin concentration within ABCG2-rich extracellular vesicles is a novel marker for multidrug resistance in malignant cells
    • Ifergan, I., V. Goler-Baron, and Y. G. Assaraf. 2009. Riboflavin concentration within ABCG2-rich extracellular vesicles is a novel marker for multidrug resistance in malignant cells. Biochem. Biophys. Res. Commun. 380:5-10.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 5-10
    • Ifergan, I.1    Goler-Baron, V.2    Assaraf, Y.G.3
  • 189
    • 0003298016 scopus 로고    scopus 로고
    • Phototropism in higher plants
    • D. P. Hader and M. Lebert (ed.), Elsevier, Amsterdam, Netherlands
    • Iino, M. 2001. Phototropism in higher plants, p. 659-811. In D. P. Hader and M. Lebert (ed.), Photomovement. Elsevier, Amsterdam, Netherlands.
    • (2001) Photomovement , pp. 659-811
    • Iino, M.1
  • 190
    • 33644519643 scopus 로고    scopus 로고
    • DNA sequencing and transcriptional analysis of the kasugamycin biosynthetic gene cluster from Streptomyces kasugaensis M338-M1
    • Tokyo
    • Ikeno, S., D. Aoki, M. Hamada, M. Hori, and K. S. Tsuchiya. 2006. DNA sequencing and transcriptional analysis of the kasugamycin biosynthetic gene cluster from Streptomyces kasugaensis M338-M1. J. Antibiot. (Tokyo) 59:18-28.
    • (2006) J. Antibiot. , vol.59 , pp. 18-28
    • Ikeno, S.1    Aoki, D.2    Hamada, M.3    Hori, M.4    Tsuchiya, K.S.5
  • 191
    • 23344450423 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B2: Diastereomeric reaction intermediates of archaeal and non-archaeal riboflavin synthases
    • Illarionov, B., W. Eisenreich, N. Schramek, A. Bacher, and M. Fischer. 2005. Biosynthesis of vitamin B2: diastereomeric reaction intermediates of archaeal and non-archaeal riboflavin synthases. J. Biol. Chem. 280:28541-28546.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28541-28546
    • Illarionov, B.1    Eisenreich, W.2    Schramek, N.3    Bacher, A.4    Fischer, M.5
  • 192
    • 0344443180 scopus 로고    scopus 로고
    • FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis
    • Imaizumi, T., H. G. Tran, T. E. Swartz, W. R. Briggs, and S. A. Kay. 2003. FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis. Nature 426:302-306.
    • (2003) Nature , vol.426 , pp. 302-306
    • Imaizumi, T.1    Tran, H.G.2    Swartz, T.E.3    Briggs, W.R.4    Kay, S.A.5
  • 193
    • 79958034530 scopus 로고
    • Nomenclature of electrontransfer proteins
    • International Union of Biochemistry. Academic Press, Orlando, FL
    • International Union of Biochemistry. 1984. Nomenclature of electrontransfer proteins. In Enzyme nomenclature, recommendations. Academic Press, Orlando, FL.
    • (1984) Enzyme Nomenclature, Recommendations
  • 194
    • 33846392721 scopus 로고    scopus 로고
    • Construction of the flavinogenic yeast Candida famata strains with high riboflavin kinase activity using gene engineering
    • In Ukrainian
    • Ishchuk, O. P., et al. 2006. Construction of the flavinogenic yeast Candida famata strains with high riboflavin kinase activity using gene engineering. Ukr. Biokhim. Zh. 78:63-69. (In Ukrainian.)
    • (2006) Ukr. Biokhim. Zh. , vol.78 , pp. 63-69
    • Ishchuk, O.P.1
  • 195
    • 38349038152 scopus 로고    scopus 로고
    • Development of a promoter assay system for the flavinogenic yeast Candida famata based on the Kluyveromyces lactis β-galactosidase LAC4 reporter gene
    • Ishchuk, O. P., et al. 2008. Development of a promoter assay system for the flavinogenic yeast Candida famata based on the Kluyveromyces lactis β-galactosidase LAC4 reporter gene. Enzyme Microb. Technol. 42:208-215.
    • (2008) Enzyme Microb. Technol. , vol.42 , pp. 208-215
    • Ishchuk, O.P.1
  • 196
    • 26844495569 scopus 로고    scopus 로고
    • Metabolic engineering of the purine pathway for riboflavin production in Ashbya gossypii
    • Jiménez, A., M. A. Santos, M. Pompejus, and J. L. Revuelta. 2005. Metabolic engineering of the purine pathway for riboflavin production in Ashbya gossypii. Appl. Environ. Microbiol. 71:5743-5751.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5743-5751
    • Jiménez, A.1    Santos, M.A.2    Pompejus, M.3    Revuelta, J.L.4
  • 197
    • 52649091290 scopus 로고    scopus 로고
    • Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii
    • Jiménez, A., M. A. Santos, and J. L. Revuelta. 2008. Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii. BMC Biotechnol. 8:67.
    • (2008) BMC Biotechnol. , vol.8 , pp. 67
    • Jiménez, A.1    Santos, M.A.2    Revuelta, J.L.3
  • 198
    • 0038690465 scopus 로고    scopus 로고
    • Yeast dihydroxybutanone phosphate synthase, an enzyme of the riboflavin biosynthetic pathway, has a second unrelated function in expression of mitochondrial respiration
    • Jin, C., A. Barrientos, and A. Tsagoloff. 2003. Yeast dihydroxybutanone phosphate synthase, an enzyme of the riboflavin biosynthetic pathway, has a second unrelated function in expression of mitochondrial respiration. J. Biol. Chem. 278:14698-14703.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14698-14703
    • Jin, C.1    Barrientos, A.2    Tsagoloff, A.3
  • 199
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans
    • Johnson, J. L., N. R. Bastian, and K. V. Rajagopalan. 1990. Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. Proc. Natl. Acad. Sci. U. S. A. 87:3190-3194.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3190-3194
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 200
    • 0033618251 scopus 로고    scopus 로고
    • Plant riboflavin biosynthesis. Cloning, chloroplast localization, expression, purification, and partial characterization of spinach lumazine synthase
    • Jordan, D. B., K. O. Bacot, T. J. Carlson, M. Kessel, and P. V. Viitanen. 1999. Plant riboflavin biosynthesis. Cloning, chloroplast localization, expression, purification, and partial characterization of spinach lumazine synthase. J. Biol. Chem. 274:22114-22121.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22114-22121
    • Jordan, D.B.1    Bacot, K.O.2    Carlson, T.J.3    Kessel, M.4    Viitanen, P.V.5
  • 202
    • 0023098376 scopus 로고
    • Formation of roseoflavin from 8-amino- And 8-methylamino-8-demethyl-D- riboflavin
    • Juri, N., et al. 1987. Formation of roseoflavin from 8-amino- and 8-methylamino-8-demethyl-D-riboflavin. J. Biochem. 101:705-711.
    • (1987) J. Biochem. , vol.101 , pp. 705-711
    • Juri, N.1
  • 203
    • 0014802798 scopus 로고
    • Pharmacokinetic evidence for saturable renal tubular reabsorption of riboflavin
    • Jusko, W. J., and G. Levy. 1970. Pharmacokinetic evidence for saturable renal tubular reabsorption of riboflavin. J. Pharm. Sci. 59:765-772.
    • (1970) J. Pharm. Sci. , vol.59 , pp. 765-772
    • Jusko, W.J.1    Levy, G.2
  • 204
    • 0013652041 scopus 로고    scopus 로고
    • Riboflavin production process by means of microorganisms with modified isocitrate lyase activity
    • January Patent WO 9703208-A
    • Kaesler, B., et al. January 1997. Riboflavin production process by means of microorganisms with modified isocitrate lyase activity. Patent WO 9703208-A.
    • (1997)
    • Kaesler, B.1
  • 205
    • 0015528055 scopus 로고
    • High-resolution proton and phosphorus nuclear magnetic resonance spectra of flavin-adenine dinucleotide and its conformation in aqueous solution
    • Kainosho, M., and Y. Kyogoku. 1972. High-resolution proton and phosphorus nuclear magnetic resonance spectra of flavin-adenine dinucleotide and its conformation in aqueous solution. Biochemistry 11:741-752.
    • (1972) Biochemistry , vol.11 , pp. 741-752
    • Kainosho, M.1    Kyogoku, Y.2
  • 206
    • 34247196744 scopus 로고    scopus 로고
    • A high-throughput screening platform for inhibitors of the riboflavin biosynthesis pathway
    • Kaiser, J., et al. 2007. A high-throughput screening platform for inhibitors of the riboflavin biosynthesis pathway. Anal. Biochem. 365:52-61.
    • (2007) Anal. Biochem. , vol.365 , pp. 52-61
    • Kaiser, J.1
  • 207
    • 0036832419 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B2
    • Kaiser, J., et al. 2002. Biosynthesis of vitamin B2. Eur. J. Biochem. 269:5264-5270.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5264-5270
    • Kaiser, J.1
  • 208
    • 0030956202 scopus 로고    scopus 로고
    • Application of agro-industrial by-products for riboflavin production by Eremothecium ashbyii NRRL 1363
    • Kalingan, A. E., and M. R. V. Krishnan. 1997. Application of agro-industrial by-products for riboflavin production by Eremothecium ashbyii NRRL 1363. Appl. Microbiol. Biotechnol. 47:226-230.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 226-230
    • Kalingan, A.E.1    Krishnan, M.R.V.2
  • 210
    • 4544372921 scopus 로고    scopus 로고
    • A genome-wide transcription analysis of a fungal riboflavin overproducer
    • Karos, M., C. Vilariño, C. Bollschweiler, and J. L. Revuelta. 2004. A genome-wide transcription analysis of a fungal riboflavin overproducer. J. Biotechnol. 113:69-76.
    • (2004) J. Biotechnol. , vol.113 , pp. 69-76
    • Karos, M.1    Vilariño, C.2    Bollschweiler, C.3    Revuelta, J.L.4
  • 212
    • 0242381351 scopus 로고    scopus 로고
    • Ligand Binding-Induced Conformational Changes in Riboflavin Kinase: Structural Basis for the Ordered Mechanism
    • DOI 10.1021/bi035450t
    • Karthikeyan, S., Q. Zhou, A. L. Osterman, and H. Zhang. 2003. Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. Biochemistry 42:12532-12538. (Pubitemid 37337543)
    • (2003) Biochemistry , vol.42 , Issue.43 , pp. 12532-12538
    • Karthikeyan, S.1    Zhou, Q.2    Osterman, A.L.3    Zhang, H.4
  • 213
    • 0018141564 scopus 로고
    • Anti-riboflavin activity of 8N-alkyl analogues of roseoflavin in some Gram-positive bacteria
    • Tokyo
    • Kasai, S., et al. 1978. Anti-riboflavin activity of 8N-alkyl analogues of roseoflavin in some Gram-positive bacteria. J. Nutr. Sci. Vitaminol. (Tokyo) 24:339-350.
    • (1978) J. Nutr. Sci. Vitaminol. , vol.24 , pp. 339-350
    • Kasai, S.1
  • 214
    • 0018722265 scopus 로고
    • Anti-riboflavin activity of 8-O-alkyl derivatives of riboflavin in some Gram-positive bacteria
    • Tokyo
    • Kasai, S., S. Yamanaka, S. C. Wang, and K. Matsui. 1979. Anti-riboflavin activity of 8-O-alkyl derivatives of riboflavin in some Gram-positive bacteria. J. Nutr. Sci. Vitaminol. (Tokyo) 25:289-298.
    • (1979) J. Nutr. Sci. Vitaminol. , vol.25 , pp. 289-298
    • Kasai, S.1    Yamanaka, S.2    Wang, S.C.3    Matsui, K.4
  • 215
    • 0017288854 scopus 로고
    • Purification and properties of the riboflavin kinase of the yeast Pichia guilliermondii
    • In Russian
    • Kashchenko, V. E., and G. M. Shavlovskii. 1976. Purification and properties of the riboflavin kinase of the yeast Pichia guilliermondii. Biokhimiia 41:376-383. (In Russian.)
    • (1976) Biokhimiia , vol.41 , pp. 376-383
    • Kashchenko, V.E.1    Shavlovskii, G.M.2
  • 217
    • 70449305045 scopus 로고
    • Biosynthesis of flavin coenzymes by microorganisms. II. Enzymatic synthesis of flavin adenine dinucleotide in Escherichia coli
    • Kyoto
    • Katagiri, H., H. Yamada, and K. Imai. 1959. Biosynthesis of flavin coenzymes by microorganisms. II. Enzymatic synthesis of flavin adenine dinucleotide in Escherichia coli. J. Vitaminol. (Kyoto) 5:307-311.
    • (1959) J. Vitaminol. , vol.5 , pp. 307-311
    • Katagiri, H.1    Yamada, H.2    Imai, K.3
  • 218
    • 33744479441 scopus 로고    scopus 로고
    • Expression of alanine:glyoxylate aminotransferase gene from Saccharomyces cerevisiae in Ashbya gossypii
    • Kato, T., and E. Y. Park. 2006. Expression of alanine:glyoxylate aminotransferase gene from Saccharomyces cerevisiae in Ashbya gossypii. Appl. Microbiol. Biotechnol. 71:46-52.
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 46-52
    • Kato, T.1    Park, E.Y.2
  • 219
    • 0011148588 scopus 로고
    • The enzymatic phosphorylation of riboflavin
    • Kearney, E. B., and S. Englard. 1951. The enzymatic phosphorylation of riboflavin. J. Biol. Chem. 193:821-834.
    • (1951) J. Biol. Chem. , vol.193 , pp. 821-834
    • Kearney, E.B.1    Englard, S.2
  • 220
    • 0018716780 scopus 로고
    • Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins
    • Kearney, E. B., J. Goldenberg, J. Lipsick, and M. Perl. 1979. Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins. J. Biol. Chem. 254:9551-9557.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9551-9557
    • Kearney, E.B.1    Goldenberg, J.2    Lipsick, J.3    Perl, M.4
  • 221
    • 0035818528 scopus 로고    scopus 로고
    • The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone- 4-phosphate synthase and ligand binding studies reveal the location of the active site
    • Kelly, M. J., et al. 2001. The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site. Proc. Natl. Acad. Sci. U. S. A. 98:13025-13030.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13025-13030
    • Kelly, M.J.1
  • 222
    • 0026632334 scopus 로고
    • Riboflavin operon of Bacillus subtilis: Unusual symmetric arrangement of the regulatory region
    • Kil, Y. V., V. N. Mironov, I. Y. Gorishin, R. A. Kreneva, and D. A. Perumov. 1992. Riboflavin operon of Bacillus subtilis: unusual symmetric arrangement of the regulatory region. Mol. Gen. Genet. 233:483-486.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 483-486
    • Kil, Y.V.1    Mironov, V.N.2    Gorishin, I.Y.3    Kreneva, R.A.4    Perumov, D.A.5
  • 223
    • 0027291929 scopus 로고
    • Purification and characterization of flavine-adenine dinucleotide phosphohydrolase from rat liver lysosomal membranes
    • Kim, J. K., J. Ezaki, M. Himeno, K. Kato, and S. Kim. 1993. Purification and characterization of flavine-adenine dinucleotide phosphohydrolase from rat liver lysosomal membranes. J. Biochem. 114:126-131. (Pubitemid 23235643)
    • (1993) Journal of Biochemistry , vol.114 , Issue.1 , pp. 126-131
    • Kim, K.S.1    Ezaki, J.2    Himeno, M.3    Kato, K.4
  • 224
    • 79958035398 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 225
    • 0029054040 scopus 로고
    • Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis
    • Kis, K., and A. Bacher. 1995. Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis. J. Biol. Chem. 270:16788-16795.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16788-16795
    • Kis, K.1    Bacher, A.2
  • 226
    • 0035917362 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. The reaction catalyzed by 6,7-dimethyl-8-ribityllumazine synthase can proceed without enzymatic catalysis under physiological conditions
    • Kis, K., K. Kugelbrey, and A. Bacher. 2001. Biosynthesis of riboflavin. The reaction catalyzed by 6,7-dimethyl-8-ribityllumazine synthase can proceed without enzymatic catalysis under physiological conditions. J. Org. Chem. 66:2555-2559.
    • (2001) J. Org. Chem. , vol.66 , pp. 2555-2559
    • Kis, K.1    Kugelbrey, K.2    Bacher, A.3
  • 227
    • 34748899957 scopus 로고    scopus 로고
    • Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales
    • Klinke, S., et al. 2007. Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales. J. Mol. Biol. 373:664-680.
    • (2007) J. Mol. Biol. , vol.373 , pp. 664-680
    • Klinke, S.1
  • 228
    • 0036146553 scopus 로고    scopus 로고
    • Reductive iron uptake by Candida albicans: Role of copper, iron and the TUP1 regulator
    • Knight, S. A., E. Lesuisse, R. Stearman, R. D. Klausner, and A. Dancis. 2002. Reductive iron uptake by Candida albicans: role of copper, iron and the TUP1 regulator. Microbiology 148:29-40. (Pubitemid 34083182)
    • (2002) Microbiology , vol.148 , Issue.1 , pp. 29-40
    • Knight, S.A.B.1    Lesuisse, E.2    Stearman, R.3    Klausner, R.D.4    Dancis, A.5
  • 229
    • 0005059567 scopus 로고
    • Biosynthesis of riboflavin in Candida guilliermondii (A. Cast) Langeron and Guerra and some related species; influence of trace elements, especially iron and zinc
    • In German
    • Knusel, F. 1957. Biosynthesis of riboflavin in Candida guilliermondii (A. Cast) Langeron and Guerra and some related species; influence of trace elements, especially iron and zinc. Arch. Mikrobiol. 27:219-259. (In German.)
    • (1957) Arch. Mikrobiol. , vol.27 , pp. 219-259
    • Knusel, F.1
  • 230
    • 0032500588 scopus 로고    scopus 로고
    • Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Kobayashi, M., et al. 1998. Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 273:26394-26399.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26394-26399
    • Kobayashi, M.1
  • 231
    • 72949129991 scopus 로고
    • Flavin adenine dinucleotide-synthesizing enzyme in Eremothecium ashbyii
    • Kyoto
    • Kobayashi, T., and T. Suzue. 1961. Flavin adenine dinucleotide- synthesizing enzyme in Eremothecium ashbyii. J. Vitaminol. (Kyoto) 7:42-47.
    • (1961) J. Vitaminol. , vol.7 , pp. 42-47
    • Kobayashi, T.1    Suzue, T.2
  • 232
    • 3242888179 scopus 로고    scopus 로고
    • Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase
    • Koch, M., et al. 2004. Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase. Eur. J. Biochem. 271:3208-3214.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3208-3214
    • Koch, M.1
  • 233
    • 0030055415 scopus 로고    scopus 로고
    • Regulation of the ribA gene encoding GTP cyclohydrolase II by the soxRS locus in Escherichia coli
    • Koh, Y. S., J. Choih, J. H. Lee, and J. H. Roe. 1996. Regulation of the ribA gene encoding GTP cyclohydrolase II by the soxRS locus in Escherichia coli. Mol. Gen. Genet. 251:591-598.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 591-598
    • Koh, Y.S.1    Choih, J.2    Lee, J.H.3    Roe, J.H.4
  • 234
    • 0033058359 scopus 로고    scopus 로고
    • The reversed SoxS-binding site upstream of the ribA promoter in Escherichia coli
    • Koh, Y. S., W. H. Chung, J. H. Lee, and J. H. Roe. 1999. The reversed SoxS-binding site upstream of the ribA promoter in Escherichia coli. Mol. Gen. Genet. 261:374-380.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 374-380
    • Koh, Y.S.1    Chung, W.H.2    Lee, J.H.3    Roe, J.H.4
  • 235
    • 0031828126 scopus 로고    scopus 로고
    • Riboflavin biosynthetic genes of Corynebacterim ammoniagenes
    • Koizumi, S., and S. Teshiba. 1998. Riboflavin biosynthetic genes of Corynebacterim ammoniagenes. J. Ferment. Bioeng. 86:130-133.
    • (1998) J. Ferment. Bioeng. , vol.86 , pp. 130-133
    • Koizumi, S.1    Teshiba, S.2
  • 236
    • 0033947879 scopus 로고    scopus 로고
    • Production of riboflavin by metabolically engineered Corynebacterium ammoniagenes
    • Koizumi, S., Y. Yonetani, A. Maruyama, and S. Teshiba. 2000. Production of riboflavin by metabolically engineered Corynebacterium ammoniagenes. Appl. Microbiol. Biotechnol. 53:674-679.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 674-679
    • Koizumi, S.1    Yonetani, Y.2    Maruyama, A.3    Teshiba, S.4
  • 237
    • 0018413097 scopus 로고
    • Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum
    • Koka, P., and J. Lee. 1979. Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum. Proc. Natl. Acad. Sci. U. S. A. 76:3068-3072.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 3068-3072
    • Koka, P.1    Lee, J.2
  • 238
    • 4644347701 scopus 로고    scopus 로고
    • The mechanism of potent GTP cyclohydrolase I inhibition by 2,4-diamino-6-hydroxypyrimidine: Requirement of the GTP cyclohydrolase I feedback regulatory protein
    • Kolinsky, M. A., and S. S. Gross. 2004. The mechanism of potent GTP cyclohydrolase I inhibition by 2,4-diamino-6-hydroxypyrimidine: requirement of the GTP cyclohydrolase I feedback regulatory protein. J. Biol. Chem. 279:40677-40682.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40677-40682
    • Kolinsky, M.A.1    Gross, S.S.2
  • 239
    • 0028057752 scopus 로고
    • Effect of pH on exocellular riboflavin production by Eremothecium ashbyii
    • Kolonne, S., R. J. Seviour, and B. M. McDougall. 1994. Effect of pH on exocellular riboflavin production by Eremothecium ashbyii. Biotechnol. Lett. 16:79-84.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 79-84
    • Kolonne, S.1    Seviour, R.J.2    McDougall, B.M.3
  • 240
    • 0021315079 scopus 로고
    • Changes in the enzyme activity of flavinogenesis in the process of culturing the fungus Eremothecium ashbyii
    • In Russian
    • Koltun, L. V., G. M. Shavlovskii, V. E. Kashchenko, and V. M. Trach. 1984. Changes in the enzyme activity of flavinogenesis in the process of culturing the fungus Eremothecium ashbyii. Mikrobiologiia 53:43-47. (In Russian.)
    • (1984) Mikrobiologiia , vol.53 , pp. 43-47
    • Koltun, L.V.1    Shavlovskii, G.M.2    Kashchenko, V.E.3    Trach, V.M.4
  • 241
    • 33646862820 scopus 로고    scopus 로고
    • Water-soluble vitamins
    • Konings, E. J. M. 2006. Water-soluble vitamins. J. AOAC Intern. 89:285-288.
    • (2006) J. AOAC Intern. , vol.89 , pp. 285-288
    • Konings, E.J.M.1
  • 243
    • 0343294372 scopus 로고    scopus 로고
    • Application of model-predictive control based on artificial neural networks to optimize the fed-batch process for riboflavin production
    • DOI 10.1016/S0168-1656(00)00211-X, PII S016816560000211X
    • Kovárová-Kovar, K., et al. 2000. Application of model-predictive control based on artificial neural networks to optimize the fed-batch process for riboflavin production. J. Biotechnol. 79:39-52. (Pubitemid 30160715)
    • (2000) Journal of Biotechnology , vol.79 , Issue.1 , pp. 39-52
    • Kovarova-Kovar, K.1    Gehlen, S.2    Kunze, A.3    Keller, T.4    Von Daniken, R.5    Kolb, M.6    Van Loon, A.P.G.M.7
  • 244
    • 0034241199 scopus 로고    scopus 로고
    • Study of the phenotypic occurrence of ypaA gene inactivation in Bacillus subtilis
    • In Russian
    • Kreneva, R. A., et al. 2000. Study of the phenotypic occurrence of ypaA gene inactivation in Bacillus subtilis. Genetika 36:1166-1168. (In Russian.)
    • (2000) Genetika , vol.36 , pp. 1166-1168
    • Kreneva, R.A.1
  • 245
    • 79958068353 scopus 로고
    • Synthetic vitamin B2
    • Kuhn, R., and F. Weygand. 1934. Synthetic vitamin B2. Berichte 67B:2084-2085.
    • (1934) Berichte , vol.67 B , pp. 2084-2085
    • Kuhn, R.1    Weygand, F.2
  • 246
    • 0345807633 scopus 로고    scopus 로고
    • Riboflavin overproduction in 4-aminopyrazole[3,4-d]pyrimidine-treated yeast Pichia guilliermondii
    • In Russian
    • Kutsiaba, V. I., N. N. Stenchuk, and D. V. Fedorovich. 2002. Riboflavin overproduction in 4-aminopyrazole[3,4-d]pyrimidine-treated yeast Pichia guilliermondii. Prikl. Biokhim. Mikrobiol. 38:268-272. (In Russian.)
    • (2002) Prikl. Biokhim. Mikrobiol. , vol.38 , pp. 268-272
    • Kutsiaba, V.I.1    Stenchuk, N.N.2    Fedorovich, D.V.3
  • 247
    • 21244452612 scopus 로고
    • On the biosynthesis of riboflavin in the culture of Eremothecium ashbyii
    • Tokyo
    • Kuwada, S., T. Masuda, T. Kishi, and M. Asai. 1958. On the biosynthesis of riboflavin in the culture of Eremothecium ashbyii. J. Vitaminol. (Tokyo) 4:217-225.
    • (1958) J. Vitaminol. , vol.4 , pp. 217-225
    • Kuwada, S.1    Masuda, T.2    Kishi, T.3    Asai, M.4
  • 248
    • 0028038142 scopus 로고
    • The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted beta-subunit capsids
    • Ladenstein, R., K. Ritsert, R. Huber, G. Richter, and A. Bacher. 1994. The lumazine synthase/riboflavin synthase complex of Bacillus subtilis. X-ray structure analysis of hollow reconstituted beta-subunit capsids. Eur. J. Biochem. 223:1007-1017.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1007-1017
    • Ladenstein, R.1    Ritsert, K.2    Huber, R.3    Richter, G.4    Bacher, A.5
  • 249
    • 0024293363 scopus 로고
    • Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the icosahedral beta 60 capsid at 3.3 A resolution
    • Ladenstein, R., et al. 1988. Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the icosahedral beta 60 capsid at 3.3 A resolution. J. Mol. Biol. 203:1045-1070.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1045-1070
    • Ladenstein, R.1
  • 251
    • 0017339844 scopus 로고
    • Utilization of analogues of riboflavin by the riboflavin-deficient chick embryo
    • Lambooy, J. P., and C. S. Shaffner. 1977. Utilization of analogues of riboflavin by the riboflavin-deficient chick embryo. J. Nutr. 107:245-250.
    • (1977) J. Nutr. , vol.107 , pp. 245-250
    • Lambooy, J.P.1    Shaffner, C.S.2
  • 252
    • 0026657443 scopus 로고
    • The lux genes in Photobacterium leiognathi are closely linked with genes corresponding in sequence to riboflavin synthesis genes
    • Lee, C. Y., and E. A. Meighen. 1992. The lux genes in Photobacterium leiognathi are closely linked with genes corresponding in sequence to riboflavin synthesis genes. Biochem. Biophys. Res. Commun. 186:690-697.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 690-697
    • Lee, C.Y.1    Meighen, E.A.2
  • 253
    • 0028265655 scopus 로고
    • Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum
    • Lee, C. Y., D. J. O'Kane, and E. A. Meighen. 1994. Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum. J. Bacteriol. 176:2100-2104.
    • (1994) J. Bacteriol. , vol.176 , pp. 2100-2104
    • Lee, C.Y.1    O'Kane, D.J.2    Meighen, E.A.3
  • 254
    • 85011936077 scopus 로고    scopus 로고
    • Roseoflavin is a natural antibacterial compound that binds to FMN riboswitches and regulates gene expression
    • Lee, E. R., K. F. Blount, and R. R. Breaker. 2009. Roseoflavin is a natural antibacterial compound that binds to FMN riboswitches and regulates gene expression. RNA Biol. 6:187-194.
    • (2009) RNA Biol. , vol.6 , pp. 187-194
    • Lee, E.R.1    Blount, K.F.2    Breaker, R.R.3
  • 255
    • 0027723765 scopus 로고
    • Lumazine protein and the excitation mechanism in bacterial bioluminescence
    • Rev.
    • Lee, J. 1993. Lumazine protein and the excitation mechanism in bacterial bioluminescence. Biophys. Chem. 48:149-158. Rev.
    • (1993) Biophys. Chem. , vol.48 , pp. 149-158
    • Lee, J.1
  • 256
    • 0022423911 scopus 로고
    • Spectral properties and function of two lumazine proteins from Photobacterium
    • Lee, J., D. J. O'Kane, and A. J. Visser. 1985. Spectral properties and function of two lumazine proteins from Photobacterium. Biochemistry 24:1476-1483.
    • (1985) Biochemistry , vol.24 , pp. 1476-1483
    • Lee, J.1    O'Kane, D.J.2    Visser, A.J.3
  • 257
    • 0031420603 scopus 로고    scopus 로고
    • Purification and characterization of 5′-nucleotidase/FAD pyrophosphatase from human placenta
    • Lee, R. S.-F., and H. C. Ford. 1997. Purification and characterization of 5′-nucleotidase/FAD pyrophosphatase from human placenta. Methods Enzymol. 280:424-436.
    • (1997) Methods Enzymol. , vol.280 , pp. 424-436
    • Lee, R.S.-F.1    Ford, H.C.2
  • 258
    • 68149170547 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Screening for an improved GTP cyclohydrolase II mutant
    • Lehmann, M., et al. 2009. Biosynthesis of riboflavin. Screening for an improved GTP cyclohydrolase II mutant. FEBS J. 276:4119-4129.
    • (2009) FEBS J. , vol.276 , pp. 4119-4129
    • Lehmann, M.1
  • 259
    • 33845187184 scopus 로고    scopus 로고
    • 2to methane in CO-grown Methanosarcina acetivorans revealed by proteomics
    • 2 to methane in CO-grown Methanosarcina acetivorans revealed by proteomics. Proc. Natl. Acad. Sci. U. S. A. 103:17921-17926.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17921-17926
    • Lessner, D.J.1
  • 260
    • 77952294811 scopus 로고    scopus 로고
    • Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD
    • Leulliot, N., et al. 2010. Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD. J. Mol. Biol. 398:641-646.
    • (2010) J. Mol. Biol. , vol.398 , pp. 641-646
    • Leulliot, N.1
  • 264
    • 0035155856 scopus 로고    scopus 로고
    • Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis
    • Liao, D. I., J. C. Calabrese, Z. Wawrzak, P. V. Viitanen, and D. B. Jordan. 2001. Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis. Structure 9:11-18.
    • (2001) Structure , vol.9 , pp. 11-18
    • Liao, D.I.1    Calabrese, J.C.2    Wawrzak, Z.3    Viitanen, P.V.4    Jordan, D.B.5
  • 265
    • 0033741195 scopus 로고    scopus 로고
    • Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe grisea
    • Liao, D. I., P. V. Viitanen, and D. B. Jordan. 2000. Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe grisea. Acta Crystallogr. D Biol. Crystallogr. 56:1495-1497.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1495-1497
    • Liao, D.I.1    Viitanen, P.V.2    Jordan, D.B.3
  • 267
    • 0029152033 scopus 로고
    • Molecular cloning of the GTP-cyclohydrolase structural gene RIB1 of Pichia guilliermondii involved in riboflavin biosynthesis
    • Liauta-Teglivets, O., M. Hasslacher, I. R. Boretskii, S. D. Kohlwein, and G. M. Shavlovskii. 1995. Molecular cloning of the GTP-cyclohydrolase structural gene RIB1 of Pichia guilliermondii involved in riboflavin biosynthesis. Yeast 11:945-952.
    • (1995) Yeast , vol.11 , pp. 945-952
    • Liauta-Teglivets, O.1    Hasslacher, M.2    Boretskii, I.R.3    Kohlwein, S.D.4    Shavlovskii, G.M.5
  • 268
    • 0016179777 scopus 로고
    • Correlation between growth and uptake of excreted riboflavin in Candida guilliermondii
    • In German
    • Liesegang, A., G. Straube, W. Fritsche, and H. Reinbothe. 1974. Correlation between growth and uptake of excreted riboflavin in Candida guilliermondii. Z. Allg. Mikrobiol. 14:691-699. (In German.)
    • (1974) Z. Allg. Mikrobiol. , vol.14 , pp. 691-699
    • Liesegang, A.1    Straube, G.2    Fritsche, W.3    Reinbothe, H.4
  • 269
    • 0442292568 scopus 로고    scopus 로고
    • Microbial production of riboflavin uasing riboflavin overproducers, Ashbya gossypii, Bacillus subtilis and Candida famata: An overview
    • Lim, S. H., J. S. Choi, and E. Y. Park. 2001. Microbial production of riboflavin uasing riboflavin overproducers, Ashbya gossypii, Bacillus subtilis and Candida famata: an overview. Biotechnol. Bioprocess Eng. 6:75-88.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 75-88
    • Lim, S.H.1    Choi, J.S.2    Park, E.Y.3
  • 270
    • 0029127546 scopus 로고
    • Association of flavin adenine dinucleotide with the Arabidopsis blue light receptor CRY1
    • Lin, C., et al. 1995. Association of flavin adenine dinucleotide with the Arabidopsis blue light receptor CRY1. Science 269:968-970.
    • (1995) Science , vol.269 , pp. 968-970
    • Lin, C.1
  • 271
    • 0034811232 scopus 로고    scopus 로고
    • Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi
    • Lin, J. W., Y. F. Chao, and S. F. Weng. 2001. Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 284:587-595.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 587-595
    • Lin, J.W.1    Chao, Y.F.2    Weng, S.F.3
  • 272
    • 77954173548 scopus 로고    scopus 로고
    • Identification of a flavin mononucleotide module residue critical for activity of inducible nitrite oxide synthase
    • Liu, X. D., T. Mazumdar, Y. Xu, E. D. Getzoff, and N. T. Eissa. 2009. Identification of a flavin mononucleotide module residue critical for activity of inducible nitrite oxide synthase. J. Immunol. 183:5977-5982.
    • (2009) J. Immunol. , vol.183 , pp. 5977-5982
    • Liu, X.D.1    Mazumdar, T.2    Xu, Y.3    Getzoff, E.D.4    Eissa, N.T.5
  • 274
    • 0023410154 scopus 로고
    • On biochemical functions of the products of genes RIB5 and RIB6 involved in riboflavin biosynthesis in the yeast Pichia guilliermondii
    • In Russian
    • Logvinenko, E. M., G. M. Shavlovskii, and N. Y. Kontorovskaya. 1987. On biochemical functions of the products of genes RIB5 and RIB6 involved in riboflavin biosynthesis in the yeast Pichia guilliermondii. Genetika 23:1699-1701. (In Russian.)
    • (1987) Genetika , vol.23 , pp. 1699-1701
    • Logvinenko, E.M.1    Shavlovskii, G.M.2    Kontorovskaya, N.Y.3
  • 275
    • 0015761997 scopus 로고
    • Role of flavins in regulating riboflavin synthetase synthesis in Pichia guilliermondii and Candida utilis
    • In Russian
    • Logvinenko, E. M., G. M. Shavlovskii, V. M. Trach, and V. A. Sibirnyi. 1973. Role of flavins in regulating riboflavin synthetase synthesis in Pichia guilliermondii and Candida utilis. Mikrobiologiia 42:1008-1014. (In Russian.)
    • (1973) Mikrobiologiia , vol.42 , pp. 1008-1014
    • Logvinenko, E.M.1    Shavlovskii, G.M.2    Trach, V.M.3    Sibirnyi, V.A.4
  • 276
    • 0024489028 scopus 로고
    • Regulation of the activity and synthesis of enzymes participating in the formation of 6,7-dimethyl-8-ribityllumazine, a riboflavin precursor in yeast
    • In Russian
    • Logvinenko, E. M., G. M. Shavlovskii, A. E. Zakalskii, and V. A. Samarskii. 1989. Regulation of the activity and synthesis of enzymes participating in the formation of 6,7-dimethyl-8-ribityllumazine, a riboflavin precursor in yeast. Ukr. Biokhim. Zhurn. 61:28-32. (In Russian.)
    • (1989) Ukr. Biokhim. Zhurn. , vol.61 , pp. 28-32
    • Logvinenko, E.M.1    Shavlovskii, G.M.2    Zakalskii, A.E.3    Samarskii, V.A.4
  • 277
    • 0019043392 scopus 로고
    • Detection of phosphorylated pyrimidine precursors of riboflavin in yeasts
    • In Russian
    • Logvinenko, E. M., G. M. Shavlovskii, A. E. Zakalskii, and E. Z. Seniuta. 1980. Detection of phosphorylated pyrimidine precursors of riboflavin in yeasts. Biokhimiia 45:1284-1292. (In Russian.)
    • (1980) Biokhimiia , vol.45 , pp. 1284-1292
    • Logvinenko, E.M.1    Shavlovskii, G.M.2    Zakalskii, A.E.3    Seniuta, E.Z.4
  • 278
    • 0020146909 scopus 로고
    • Biosynthesis of 6,7-dimethyl-8-ribityllumazine in the extracts of the yeast Pichia guilliermondii
    • In Russian
    • Logvinenko, E. M., G. M. Shavlovskii, A. E. Zakalskii, and I. V. Zakhodylo. 1982. Biosynthesis of 6,7-dimethyl-8-ribityllumazine in the extracts of the yeast Pichia guilliermondii. Biokhimiia 47:931-936. (In Russian.)
    • (1982) Biokhimiia , vol.47 , pp. 931-936
    • Logvinenko, E.M.1    Shavlovskii, G.M.2    Zakalskii, A.E.3    Zakhodylo, I.V.4
  • 279
    • 0027339005 scopus 로고
    • Cloning of the RIB7 gene encoding the riboflavin synthase of the yeast Pichia guilliermondii
    • In Russian
    • Logvinenko, E. M., et al. 1993. Cloning of the RIB7 gene encoding the riboflavin synthase of the yeast Pichia guilliermondii. Genetika 29:922-927. (In Russian.)
    • (1993) Genetika , vol.29 , pp. 922-927
    • Logvinenko, E.M.1
  • 280
    • 77449123790 scopus 로고    scopus 로고
    • Riboflavin biosynthetic and regulatory factors as potential novel anti-infective drug targets
    • Long, Q., L. Ji, H. Wang, and J. Xie. 2010. Riboflavin biosynthetic and regulatory factors as potential novel anti-infective drug targets. Chem. Biol. Drug Des. 75:339-347.
    • (2010) Chem. Biol. Drug Des. , vol.75 , pp. 339-347
    • Long, Q.1    Ji, L.2    Wang, H.3    Xie, J.4
  • 281
    • 33745488371 scopus 로고    scopus 로고
    • Riboflavin analogs and inhibitors of riboflavin biosynthesis
    • Mack, M., and S. Grill. 2006. Riboflavin analogs and inhibitors of riboflavin biosynthesis. Appl. Microbiol. Biotechnol. 71:265-275.
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 265-275
    • Mack, M.1    Grill, S.2
  • 282
    • 0031882942 scopus 로고    scopus 로고
    • Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC
    • Mack, M., A. P. van Loon, and H. P. Hohmann. 1998. Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC. J. Bacteriol. 180:950-955.
    • (1998) J. Bacteriol. , vol.180 , pp. 950-955
    • Mack, M.1    Van Loon, A.P.2    Hohmann, H.P.3
  • 283
    • 45749137952 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis
    • Magalhães, M. L., A. Argyrou, S. M. Cahill, and J. S. Blanchard. 2008. Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis. Biochemistry 47:6499-6507.
    • (2008) Biochemistry , vol.47 , pp. 6499-6507
    • Magalhães, M.L.1    Argyrou, A.2    Cahill, S.M.3    Blanchard, J.S.4
  • 284
    • 0017127225 scopus 로고
    • Biosynthesis of riboflavin. Structure of the purine precursor and origin of the ribityl side chain
    • Mailänder, B., and A. Bacher. 1976. Biosynthesis of riboflavin. Structure of the purine precursor and origin of the ribityl side chain. J. Biol. Chem. 251:3623-3628.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3623-3628
    • Mailänder, B.1    Bacher, A.2
  • 285
    • 10944238494 scopus 로고    scopus 로고
    • Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein
    • Maita, N., K. Hatakeyama, K. Okada, and T. Hakoshima. 2004. Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein. J. Biol. Chem. 279:51534-51540.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51534-51540
    • Maita, N.1    Hatakeyama, K.2    Okada, K.3    Hakoshima, T.4
  • 286
    • 0013495946 scopus 로고
    • The isolation, synthesis, and metabolic properties of 6,7-dimethyl-8-ribityllumazine
    • Maley, G. F., and G. W. Plaut. 1959. The isolation, synthesis, and metabolic properties of 6,7-dimethyl-8-ribityllumazine. J. Biol. Chem. 234:641-647.
    • (1959) J. Biol. Chem. , vol.234 , pp. 641-647
    • Maley, G.F.1    Plaut, G.W.2
  • 287
    • 33846452511 scopus 로고    scopus 로고
    • The bile/arsenite/riboflavin transporter (BART) superfamily
    • Mansour, N. M., M. Sawhney, D. G. Tamang, C. Vogl, and M. H. Saier, Jr. 2007. The bile/arsenite/riboflavin transporter (BART) superfamily. FEBS J. 274:612-629.
    • (2007) FEBS J. , vol.274 , pp. 612-629
    • Mansour, N.M.1    Sawhney, M.2    Tamang, D.G.3    Vogl, C.4    Saier Jr., M.H.5
  • 288
    • 0022970597 scopus 로고
    • Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes
    • Manstein, D. J., and E. F. Pai. 1986. Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes. J. Biol. Chem. 261:16169-16173.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16169-16173
    • Manstein, D.J.1    Pai, E.F.2
  • 289
    • 41649085415 scopus 로고    scopus 로고
    • Shewanella secretes flavins that mediate extracellular electron transfer
    • Marsili, E., et al. 2008. Shewanella secretes flavins that mediate extracellular electron transfer. Proc. Natl. Acad. Sci. U. S. A. 105:3968-3973.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3968-3973
    • Marsili, E.1
  • 290
    • 49949115796 scopus 로고    scopus 로고
    • Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris
    • Marx, H., D. Mattanovich, and M. Sauer. 2008. Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris. Microb. Cell Fact. 7:23.
    • (2008) Microb. Cell Fact. , vol.7 , pp. 23
    • Marx, H.1    Mattanovich, D.2    Sauer, M.3
  • 291
    • 41549136541 scopus 로고    scopus 로고
    • Identification and characterization of an archaeon-specific riboflavin kinase
    • Mashhadi, Z., H. Zhang, H. Xu, and R. H. White. 2008. Identification and characterization of an archaeon-specific riboflavin kinase. J. Bacteriol. 190:2615-2618.
    • (2008) J. Bacteriol. , vol.190 , pp. 2615-2618
    • Mashhadi, Z.1    Zhang, H.2    Xu, H.3    White, R.H.4
  • 292
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versality of riboflavin
    • Massey, V. 2000. The chemical and biological versality of riboflavin. Biochem. Soc. Trans. 28:283-296.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 293
    • 77049253130 scopus 로고
    • Application of chromatography. XXVIII. On the formation of FAD in the culture of Eremothecium ashbyii
    • Masuda, T. 1955. Application of chromatography. XXVIII. On the formation of FAD in the culture of Eremothecium ashbyii. Pharm. Bull. 3:434-440.
    • (1955) Pharm. Bull. , vol.3 , pp. 434-440
    • Masuda, T.1
  • 294
    • 33746049809 scopus 로고    scopus 로고
    • Purine biosynthesis, riboflavin production, and trophic-phase span are controlled by a Myb-related transcription factor in the fungus Ashbya gossypii
    • Mateos, L., A. Jiménez, J. L. Revuelta, and M. A. Santos. 2006. Purine biosynthesis, riboflavin production, and trophic-phase span are controlled by a Myb-related transcription factor in the fungus Ashbya gossypii. Appl. Environ. Microbiol. 72:5052-5060.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5052-5060
    • Mateos, L.1    Jiménez, A.2    Revuelta, J.L.3    Santos, M.A.4
  • 295
    • 58549088979 scopus 로고    scopus 로고
    • In vivo generation of flavoproteins with modified cofactors
    • Mathes, T., C. Vogl, J. Stolz, and P. Hegemann. 2009. In vivo generation of flavoproteins with modified cofactors. J. Mol. Biol. 385:1511-1518.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1511-1518
    • Mathes, T.1    Vogl, C.2    Stolz, J.3    Hegemann, P.4
  • 296
    • 0017652033 scopus 로고
    • Mutation of an inosine-producing strain of Bacillus subtilis to DL-methionine sulfoxide resistance for guanosine production
    • Matsui, H., K. Sato, H. Enei, and Y. Hirose. 1977. Mutation of an inosine-producing strain of Bacillus subtilis to DL-methionine sulfoxide resistance for guanosine production. Appl. Environ. Microbiol. 34:337-341.
    • (1977) Appl. Environ. Microbiol. , vol.34 , pp. 337-341
    • Matsui, H.1    Sato, K.2    Enei, H.3    Hirose, Y.4
  • 297
    • 0018589037 scopus 로고
    • Production of guanosine by psicofuranine and decoyinine resistant mutants of Bacillus subtilis
    • Matsui, H., K. Sato, H. Enei, and Y. Hirose. 1979. Production of guanosine by psicofuranine and decoyinine resistant mutants of Bacillus subtilis. Agric. Biol. Chem. 43:1739-1744.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 1739-1744
    • Matsui, H.1    Sato, K.2    Enei, H.3    Hirose, Y.4
  • 298
    • 0018286917 scopus 로고
    • Formation of roseoflavin from guanine through riboflavin
    • Matsui, K., N. Juri, Y. Kubo, and S. Kasai. 1979. Formation of roseoflavin from guanine through riboflavin. J. Biochem. 86:167-175. (Pubitemid 9242994)
    • (1979) Journal of Biochemistry , vol.86 , Issue.1 , pp. 167-175
    • Matsui, K.1    Juri, N.2    Kubo, Y.3    Kasai, S.4
  • 299
    • 0029944854 scopus 로고    scopus 로고
    • Identification of nektoflavin as 7-alphahydroxy-riboflavin
    • Matsui, K., and S. Kasai. 1996. Identification of nektoflavin as 7-alphahydroxy-riboflavin. J. Biochem. 119:441-447.
    • (1996) J. Biochem. , vol.119 , pp. 441-447
    • Matsui, K.1    Kasai, S.2
  • 300
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. 2006. To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31:276-283.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 303
    • 0015637301 scopus 로고
    • Inhibition of dihydropteroate synthetase from Escherichia coli by sulfones and sulfonamides
    • McCullough, J. L., and T. H. Maren. 1973. Inhibition of dihydropteroate synthetase from Escherichia coli by sulfones and sulfonamides. Antimicrob. Agents Chemother. 3:665-669.
    • (1973) Antimicrob. Agents Chemother. , vol.3 , pp. 665-669
    • McCullough, J.L.1    Maren, T.H.2
  • 304
    • 0027319251 scopus 로고
    • Bacterial bioluminescence: Organization, regulation, and application of the lux genes
    • Meighen, E. A. 1993. Bacterial bioluminescence: organization, regulation, and application of the lux genes. FASEB J. 7:1016-1022. (Pubitemid 23243443)
    • (1993) FASEB Journal , vol.7 , Issue.11 , pp. 1016-1022
    • Meighen, E.A.1
  • 305
    • 0034716938 scopus 로고    scopus 로고
    • The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 A resolution reveals the binding mode of a phosphonate intermediate analogue
    • Meining, W., et al. 2000. The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 A resolution reveals the binding mode of a phosphonate intermediate analogue. J. Mol. Biol. 299:181-197.
    • (2000) J. Mol. Biol. , vol.299 , pp. 181-197
    • Meining, W.1
  • 306
    • 0028880974 scopus 로고
    • Sequences of ribosomal genes and internal transcribed spacers move three plant parasitic fungi, Eremothecium ashbyi, Ashbya gossypii, and Nematospora coryli, towards Saccharomyces cerevisiae
    • Messner, R., H. J. Prillinger, M. Ibl, and G. Himmler. 1995. Sequences of ribosomal genes and internal transcribed spacers move three plant parasitic fungi, Eremothecium ashbyi, Ashbya gossypii, and Nematospora coryli, towards Saccharomyces cerevisiae. J. Gen. Appl. Microbiol. 41:31-42.
    • (1995) J. Gen. Appl. Microbiol. , vol.41 , pp. 31-42
    • Messner, R.1    Prillinger, H.J.2    Ibl, M.3    Himmler, G.4
  • 307
    • 0018188715 scopus 로고
    • Origin of the ribityl side-chain of riboflavin from the ribose moiety of guanosine triphosphate in Pichia guilliermondii yeast
    • Miersch, J., E. M. Logvinenko, A. E. Zakalsky, G. M. Shavlovsky, and H. Reinbothe. 1978. Origin of the ribityl side-chain of riboflavin from the ribose moiety of guanosine triphosphate in Pichia guilliermondii yeast. Biochim. Biophys. Acta 543:305-312.
    • (1978) Biochim. Biophys. Acta , vol.543 , pp. 305-312
    • Miersch, J.1    Logvinenko, E.M.2    Zakalsky, A.E.3    Shavlovsky, G.M.4    Reinbothe, H.5
  • 308
    • 0035844170 scopus 로고    scopus 로고
    • NADH oxidase activity of mitochondrial apoptosis-inducing factor
    • Miramar, M. D., et al. 2001. NADH oxidase activity of mitochondrial apoptosis-inducing factor. J. Biol. Chem. 276:16391-16398.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16391-16398
    • Miramar, M.D.1
  • 310
    • 0028044897 scopus 로고
    • Functional organization of the riboflavin biosynthesis operon from Bacillus subtilis SHgw
    • Mironov, V. N., et al. 1994. Functional organization of the riboflavin biosynthesis operon from Bacillus subtilis SHgw. Mol. Gen. Genet. 242:201-208.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 201-208
    • Mironov, V.N.1
  • 311
    • 0025093440 scopus 로고
    • Unusual structure of the regulatory region of the riboflavin biosynthesis operon in Bacillus subtilis
    • Moscow
    • Mironov, V. N., D. A. Perumov, A. S. Kraev, A. I. Stepanov, and K. G. Skriabin. 1990. Unusual structure of the regulatory region of the riboflavin biosynthesis operon in Bacillus subtilis. Mol. Biol. (Moscow) 24:256-261.
    • (1990) Mol. Biol. , vol.24 , pp. 256-261
    • Mironov, V.N.1    Perumov, D.A.2    Kraev, A.S.3    Stepanov, A.I.4    Skriabin, K.G.5
  • 312
    • 34447109298 scopus 로고
    • Studies on plant flavokinase. II. The purification and some properties of bean flavokinase
    • Tokyo
    • Mitsuda, H., Y. Tomozawa, and F. Kawai. 1963. Studies on plant flavokinase. II. The purification and some properties of bean flavokinase. J. Vitaminol. (Tokyo) 66:142-148.
    • (1963) J. Vitaminol. , vol.66 , pp. 142-148
    • Mitsuda, H.1    Tomozawa, Y.2    Kawai, F.3
  • 313
    • 0035749742 scopus 로고    scopus 로고
    • Versatility and specificity in flavoenzymes: Control mechanisms of flavin reactivity
    • Miura, R. 2001. Versatility and specificity in flavoenzymes: control mechanisms of flavin reactivity. Chem. Rec. 1:183-194.
    • (2001) Chem. Rec. , vol.1 , pp. 183-194
    • Miura, R.1
  • 314
    • 0031734351 scopus 로고    scopus 로고
    • Threonine aldolase overexpression plus threonine supplementation enhanced riboflavin production in Ashbya gossypii
    • Monschau, N., H. Sahm, and K. P. Stahmann. 1998. Threonine aldolase overexpression plus threonine supplementation enhanced riboflavin production in Ashbya gossypii. Appl. Environ. Microbiol. 64:4283-4290.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4283-4290
    • Monschau, N.1    Sahm, H.2    Stahmann, K.P.3
  • 316
    • 33749389011 scopus 로고    scopus 로고
    • Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis
    • DOI 10.1111/j.1742-4658.2006.05481.x
    • Morgunova, E., et al. 2006. Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis. FEBS J. 273:4790-4804. (Pubitemid 44506915)
    • (2006) FEBS Journal , vol.273 , Issue.20 , pp. 4790-4804
    • Morgunova, E.1    Illarionov, B.2    Sambaiah, T.3    Haase, I.4    Bacher, A.5    Cushman, M.6    Fischer, M.7    Ladenstein, R.8
  • 317
    • 14344262526 scopus 로고    scopus 로고
    • Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: Binding mode of a new class of purinetrione inhibitors
    • DOI 10.1021/bi047848a
    • Morgunova, E., et al. 2005. Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors. Biochemistry 44:2746-2758. (Pubitemid 40293651)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2746-2758
    • Morgunova, E.1    Meining, W.2    Illarionov, B.3    Haase, I.4    Jin, G.5    Bacher, A.6    Cushman, M.7    Fischer, M.8    Ladenstein, R.9
  • 318
    • 34447126343 scopus 로고    scopus 로고
    • Lumazine synthase from Candida albicans as an anti-fungal target enzyme: Structural and biochemical basis for drug design
    • Morgunova, E., et al. 2007. Lumazine synthase from Candida albicans as an anti-fungal target enzyme: structural and biochemical basis for drug design. J. Biol. Chem. 282:17231-17241.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17231-17241
    • Morgunova, E.1
  • 319
    • 0031435281 scopus 로고    scopus 로고
    • A novel process of inosine 5′-monophosphate production using overexpressed guanosine/inosine kinase
    • Mori, H., A. Iida, T. Fujio, and S. Teshiba. 1997. A novel process of inosine 5′-monophosphate production using overexpressed guanosine/inosine kinase. Appl. Microbiol. Biotechnol. 48:693-698.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 693-698
    • Mori, H.1    Iida, A.2    Fujio, T.3    Teshiba, S.4
  • 320
    • 0030451820 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli
    • Mörtl, S., et al. 1996. Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli. J. Biol. Chem. 271:33201-33327.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33201-33327
    • Mörtl, S.1
  • 321
    • 0005085985 scopus 로고
    • Effect of copper and zinc deficiency on the synthesis of protein and riboflavin by Aspergillus niger
    • Naik, M. S., and N. B. Das. 1964. Effect of copper and zinc deficiency on the synthesis of protein and riboflavin by Aspergillus niger. Indian J. Exp. Biol. 2:59-64.
    • (1964) Indian J. Exp. Biol. , vol.2 , pp. 59-64
    • Naik, M.S.1    Das, N.B.2
  • 322
    • 85007873382 scopus 로고
    • Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli
    • Nakagawa, S., et al. 1995. Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli. Biosci. Biotechnol. Biochem. 59:694-702.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 694-702
    • Nakagawa, S.1
  • 323
    • 0023225568 scopus 로고
    • Termination of pregnancy in mice with antiserum to chicken riboflavin-carrier protein
    • Natraj, U., R. A. Kumar, and P. Kadam. 1987. Termination of pregnancy in mice with antiserum to chicken riboflavin-carrier protein. Biol. Reprod. 36:677-685.
    • (1987) Biol. Reprod. , vol.36 , pp. 677-685
    • Natraj, U.1    Kumar, R.A.2    Kadam, P.3
  • 324
    • 65549098694 scopus 로고    scopus 로고
    • Differentiation of Debaryomyces hansenii and Candida famata by rRNA gene intergenic spacer fingerprinting and reassessment of phylogenetic relationships among D. hansenii, C. famata, D. fabryi, C. flareri (=D. subglobosus) and D. prosopidis: Description of D. vietnamensis sp. nov. closely related to D. nepalensis
    • Nguyen, H. V., C. Gaillardin, and C. Neuvéglise. 2009. Differentiation of Debaryomyces hansenii and Candida famata by rRNA gene intergenic spacer fingerprinting and reassessment of phylogenetic relationships among D. hansenii, C. famata, D. fabryi, C. flareri (=D. subglobosus) and D. prosopidis: description of D. vietnamensis sp. nov. closely related to D. nepalensis. FEMS Yeast Res. 9:641-662.
    • (2009) FEMS Yeast Res. , vol.9 , pp. 641-662
    • Nguyen, H.V.1    Gaillardin, C.2    Neuvéglise, C.3
  • 325
    • 0019807080 scopus 로고
    • Biosynthesis of riboflavin. Characterization of the product of the deaminase
    • Nielsen, P., and A. Bacher. 1981. Biosynthesis of riboflavin. Characterization of the product of the deaminase. Biochim. Biophys. Acta 662:312-317.
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 312-317
    • Nielsen, P.1    Bacher, A.2
  • 326
    • 0020626246 scopus 로고
    • Phosphates of riboflavin and riboflavin analogs: A reinvestigation by high-performance liquid chromatography
    • Nielsen, P., P. Rauschenbach, and A. Bacher. 1983. Phosphates of riboflavin and riboflavin analogs: a reinvestigation by high-performance liquid chromatography. Anal. Biochem. 130:359-368.
    • (1983) Anal. Biochem. , vol.130 , pp. 359-368
    • Nielsen, P.1    Rauschenbach, P.2    Bacher, A.3
  • 327
    • 0346687595 scopus 로고    scopus 로고
    • The riboswitch control of bacterial metabolism
    • Nudler, E., and A. S. Mironov. 2004. The riboswitch control of bacterial metabolism. Trends Biochem. Sci. 29:11-17.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 11-17
    • Nudler, E.1    Mironov, A.S.2
  • 328
    • 0020630875 scopus 로고
    • New metabolites of riboflavin appear in human purine
    • Ohkawa, H., N. Ohnishi, and K. Yagi. 1983. New metabolites of riboflavin appear in human purine. J. Biol. Chem. 258:5623-5628.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5623-5628
    • Ohkawa, H.1    Ohnishi, N.2    Yagi, K.3
  • 329
    • 0023664455 scopus 로고
    • Complete purification and general characterization of FAD synthetase from rat liver
    • Oka, M., and D. B. McCormick. 1987. Complete purification and general characterization of FAD synthetase from rat liver. J. Biol. Chem. 262:7418-7422.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7418-7422
    • Oka, M.1    McCormick, D.B.2
  • 331
    • 0017872950 scopus 로고
    • n-Alkanes as a substratum for riboflavin production. I. Investigations of the dynamics of the flavinogenesis in chosen yeasts of the genus Candida
    • Olczyk, C. 1978. n-Alkanes as a substratum for riboflavin production. I. Investigations of the dynamics of the flavinogenesis in chosen yeasts of the genus Candida. Pol. J. Pharmacol. Pharm. 30:83-88.
    • (1978) Pol. J. Pharmacol. Pharm. , vol.30 , pp. 83-88
    • Olczyk, C.1
  • 332
    • 0015351687 scopus 로고
    • Biosynthesis of riboflavine in Saccharomyces cerevisiae: The role of genes rib1 and rib7
    • Oltmanns, O., and A. Bacher. 1972. Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes rib1 and rib7. J. Bacteriol. 110:818-822.
    • (1972) J. Bacteriol. , vol.110 , pp. 818-822
    • Oltmanns, O.1    Bacher, A.2
  • 333
    • 0014642157 scopus 로고
    • Biochemical and genetic classification of riboflavine deficient mutants of Saccharomyces cerevisiae
    • Oltmanns, O., A. Bacher, F. Lingens, and F. K. Zimmermann. 1969. Biochemical and genetic classification of riboflavine deficient mutants of Saccharomyces cerevisiae. Mol. Gen. Genet. 105:306-313.
    • (1969) Mol. Gen. Genet. , vol.105 , pp. 306-313
    • Oltmanns, O.1    Bacher, A.2    Lingens, F.3    Zimmermann, F.K.4
  • 334
    • 0032516906 scopus 로고    scopus 로고
    • Cloning and analysis of the genes for a novel electron-transferring flavoprotein from Megasphaera elsdenii. Expression and characterization of the recombinant protein
    • O'Neill, H., S. G. Mayhew, and G. Butler. 1998. Cloning and analysis of the genes for a novel electron-transferring flavoprotein from Megasphaera elsdenii. Expression and characterization of the recombinant protein. J. Biol. Chem. 273:21015-21024.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21015-21024
    • O'Neill, H.1    Mayhew, S.G.2    Butler, G.3
  • 335
    • 77949488919 scopus 로고
    • Studies on roseoflavin: Isolation, physical, chemical and biological properties
    • T. P. Singer (ed.), Elsevier Scientific Publishing Co., Amsterdam, Netherlands
    • Otani, S. 1976. Studies on roseoflavin: isolation, physical, chemical and biological properties, p. 323-327. In T. P. Singer (ed.), Flavins and flavoproteins. Elsevier Scientific Publishing Co., Amsterdam, Netherlands.
    • (1976) Flavins and Flavoproteins , pp. 323-327
    • Otani, S.1
  • 336
    • 0016000179 scopus 로고
    • Roseoflavin, a new antimicrobial pigment from Streptomyces
    • Tokyo
    • Otani, S., M. Takatsu, M. Nakano, S. Kasa, and R. Miura. 1974. Roseoflavin, a new antimicrobial pigment from Streptomyces. J. Antibiot. (Tokyo) 27:86-87.
    • (1974) J. Antibiot. , vol.27 , pp. 86-87
    • Otani, S.1    Takatsu, M.2    Nakano, M.3    Kasa, S.4    Miura, R.5
  • 337
    • 67650474303 scopus 로고    scopus 로고
    • The RFN riboswitch of Bacillus subtilis is a target for the antibiotic roseoflavin produced by Streptomyces davawensis
    • Ott, E. J. Stolz, M. Lehmann, and M. Mack. 2009. The RFN riboswitch of Bacillus subtilis is a target for the antibiotic roseoflavin produced by Streptomyces davawensis. RNA Biol. 6:276-280.
    • (2009) RNA Biol. , vol.6 , pp. 276-280
    • Ott, E.1    Stolz, J.2    Lehmann, M.3    Mack, M.4
  • 338
    • 0022586432 scopus 로고
    • Riboflavin production by Eremothecium ashbyii in a batch stirred tank fermentor
    • Özbas, T., and T. Kutsal. 1986. Riboflavin production by Eremothecium ashbyii in a batch stirred tank fermentor. Biotechnol. Lett. 8:441-444.
    • (1986) Biotechnol. Lett. , vol.8 , pp. 441-444
    • Özbas, T.1    Kutsal, T.2
  • 339
    • 0022997215 scopus 로고
    • Comparative study of riboflavin production by two organisms Eremothecium ashbyii and Ashbya gossypii
    • Özbas, T., and T. Kutsal. 1986. Comparative study of riboflavin production by two organisms Eremothecium ashbyii and Ashbya gossypii. Enzyme Microb. Technol. 3:593-596.
    • (1986) Enzyme Microb. Technol. , vol.3 , pp. 593-596
    • Özbas, T.1    Kutsal, T.2
  • 340
    • 27644453559 scopus 로고    scopus 로고
    • Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein
    • DOI 10.1016/j.femsyr.2005.06.005, PII S1567135605001182
    • Ozimek, P., M. Veenhuis, and I. J. van der Klei. 2005. Alcohol oxidase: a complex peroxisomal, oligomeric flavoprotein. FEMS Yeast Res. 5:975-983. (Pubitemid 41564051)
    • (2005) FEMS Yeast Research , vol.5 , Issue.11 , pp. 975-983
    • Ozimek, P.1    Veenhuis, M.2    Van Der, K.I.J.3
  • 341
    • 34447505085 scopus 로고    scopus 로고
    • Isolation of Ashbya gossypii mutant for an improved riboflavin production targeting for biorefinery technology
    • Park, E. Y., J. H. Zhang, S. Tajima, and L. Dwiarti. 2007. Isolation of Ashbya gossypii mutant for an improved riboflavin production targeting for biorefinery technology. J. Appl. Microbiol. 103:468-476.
    • (2007) J. Appl. Microbiol. , vol.103 , pp. 468-476
    • Park, E.Y.1    Zhang, J.H.2    Tajima, S.3    Dwiarti, L.4
  • 342
    • 0015268040 scopus 로고
    • The biosynthesis of pteridines. VI. Studies of the mechanism of riboflavin biosynthesis
    • Paterson, T., and H. C. Wood. 1972. The biosynthesis of pteridines. VI. Studies of the mechanism of riboflavin biosynthesis. J. Chem. Soc. Perkin 1 8:1051-1056.
    • (1972) J. Chem. Soc. Perkin 1 , vol.8 , pp. 1051-1056
    • Paterson, T.1    Wood, H.C.2
  • 344
    • 0008096946 scopus 로고
    • Riboflavin overproducing strains of bacteria
    • January European patent EP 0 405 370 B2
    • Perkins, J. B., J. G. Pero, and A. Sloma. January 1991. Riboflavin overproducing strains of bacteria. European patent EP 0 405 370 B2.
    • (1991)
    • Perkins, J.B.1    Pero, J.G.2    Sloma, A.3
  • 345
    • 0032993682 scopus 로고    scopus 로고
    • Genetic engineering of Bacillus subtilis for the commercial production of riboflavin
    • Perkins, J. B., et al. 1999. Genetic engineering of Bacillus subtilis for the commercial production of riboflavin. J. Ind. Microbiol. Biotechnol. 22:8-18.
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.22 , pp. 8-18
    • Perkins, J.B.1
  • 346
    • 34548301837 scopus 로고    scopus 로고
    • Bacterial strains which overproduce riboflavin
    • July U.S. patent 5,925,538
    • Perkins, J. B., et al. July 1999. Bacterial strains which overproduce riboflavin. U.S. patent 5,925,538.
    • (1999)
    • Perkins, J.B.1
  • 347
    • 0017153639 scopus 로고
    • Transport of riboflavin into yeast cells
    • Perl, M., E. B. Kearney, and T. P. Singer. 1976. Transport of riboflavin into yeast cells. J. Biol. Chem. 251:3221-3228.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3221-3228
    • Perl, M.1    Kearney, E.B.2    Singer, T.P.3
  • 348
    • 0032725195 scopus 로고    scopus 로고
    • Crystal structure analysis of a pentameric fungal and an icosahedral plant lumazine synthase reveals the structural basis for differences in assembly
    • Persson, K., G. Schneider, D. B. Jordan, P. V. Viitanen, and T. Sandalova. 1999. Crystal structure analysis of a pentameric fungal and an icosahedral plant lumazine synthase reveals the structural basis for differences in assembly. Protein Sci. 8:2355-2365. (Pubitemid 29536401)
    • (1999) Protein Science , vol.8 , Issue.11 , pp. 2355-2365
    • Persson, K.1    Schneider, G.2    Jordan, D.B.3    Viitanen, P.V.4    Sandalova, T.5
  • 349
    • 0029084746 scopus 로고
    • Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11
    • Peschke, U., H. Schmidt, H. Z. Zhang, and W. Piepersberg. 1995. Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11. Mol. Microbiol. 16:1137-1156.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1137-1156
    • Peschke, U.1    Schmidt, H.2    Zhang, H.Z.3    Piepersberg, W.4
  • 350
    • 79958053527 scopus 로고
    • Lactoflavin in microorganisms
    • Pett, T. 1936. Lactoflavin in microorganisms. Biochem. J. 30:1438.
    • (1936) Biochem. J. , vol.30 , pp. 1438
    • Pett, T.1
  • 351
    • 0030982185 scopus 로고    scopus 로고
    • Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1
    • Petushkov, V. N., and J. Lee. 1997. Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1. Eur. J. Biochem. 245:790-796.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 790-796
    • Petushkov, V.N.1    Lee, J.2
  • 352
    • 22544438442 scopus 로고    scopus 로고
    • Homologues of yeast polarity genes control the development of multinucleated hyphae in Ashbya gossypii
    • Philippsen, P., A. Kaufmann, and H. P. Schmitz. 2005. Homologues of yeast polarity genes control the development of multinucleated hyphae in Ashbya gossypii. Curr. Opin. Microbiol. 8:370-377.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 370-377
    • Philippsen, P.1    Kaufmann, A.2    Schmitz, H.P.3
  • 353
    • 0015918381 scopus 로고
    • Genetics of resistance to 4-aminopyrazolo-(3,4-d)-pyrimidine in Saccharomyces cerevisiae
    • Pickering, W. R., and R. A. Woods. 1973. Genetics of resistance to 4-aminopyrazolo-(3,4-d)-pyrimidine in Saccharomyces cerevisiae. Mol. Gen. Genet. 122:231-242.
    • (1973) Mol. Gen. Genet. , vol.122 , pp. 231-242
    • Pickering, W.R.1    Woods, R.A.2
  • 354
    • 0001976613 scopus 로고
    • Studies on the stoichiometry of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin
    • Plaut, G. W. 1960. Studies on the stoichiometry of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin. J. Biol. Chem. 235:PC41-PC42.
    • (1960) J. Biol. Chem. , vol.235
    • Plaut, G.W.1
  • 355
    • 0001653222 scopus 로고
    • Studies on the nature of the enzymic conversion of 6,7-dimethyl-8- ribityllumazine to riboflavin
    • Plaut, G. W. 1963. Studies on the nature of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin. J. Biol. Chem. 238:2225-2243.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2225-2243
    • Plaut, G.W.1
  • 356
    • 0002594258 scopus 로고
    • M. Florkin and E. H. Stolz (ed.), Elsevier, Amsterdam, Netherlands
    • Plaut, G. W. E. 1971. The biosynthesis of riboflavin, p. 11-45. In M. Florkin and E. H. Stolz (ed.), Elsevier, Amsterdam, Netherlands.
    • (1971) The Biosynthesis of Riboflavin , pp. 11-45
    • Plaut, G.W.E.1
  • 357
    • 0014952520 scopus 로고
    • Studies on the mechanism of elimination of protons from the methyl groups of 6,7-dimethyl-8-ribityllumazine by riboflavin synthetase
    • Plaut, G. W., R. L. Beach, and T. Aogaichi. 1970. Studies on the mechanism of elimination of protons from the methyl groups of 6,7-dimethyl-8-ribityllumazine by riboflavin synthetase. Biochemistry 9:771-785.
    • (1970) Biochemistry , vol.9 , pp. 771-785
    • Plaut, G.W.1    Beach, R.L.2    Aogaichi, T.3
  • 358
    • 0037563951 scopus 로고    scopus 로고
    • Riboflavin (vitamin B-2) and health
    • Powers, H. J. 2003. Riboflavin (vitamin B-2) and health. Am. J. Clin. Nutr. 77:1352-1360.
    • (2003) Am. J. Clin. Nutr. , vol.77 , pp. 1352-1360
    • Powers, H.J.1
  • 359
    • 0034149737 scopus 로고    scopus 로고
    • Oversynthesis of riboflavin by yeast Pichia guilliermondii in response to oxidative stress
    • Protchenko, O. V., Y. R. Boretsky, T. M. Romanyuk, and D. V. Fedorovych. 2000. Oversynthesis of riboflavin by yeast Pichia guilliermondii in response to oxidative stress. Ukr. Biokhim. Zh. 72:19-23.
    • (2000) Ukr. Biokhim. Zh. , vol.72 , pp. 19-23
    • Protchenko, O.V.1    Boretsky, Y.R.2    Romanyuk, T.M.3    Fedorovych, D.V.4
  • 360
    • 33746356213 scopus 로고    scopus 로고
    • A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum
    • Protchenko, O., R. Rodriguez-Suarez, R. Androphy, H. Bussey, and C. C. Philpott. 2006. A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum. J. Biol. Chem. 281:21445-21457.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21445-21457
    • Protchenko, O.1    Rodriguez-Suarez, R.2    Androphy, R.3    Bussey, H.4    Philpott, C.C.5
  • 361
    • 0029961610 scopus 로고    scopus 로고
    • 420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis
    • 420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis. J. Bacteriol. 178:2861-2866.
    • (1996) J. Bacteriol. , vol.178 , pp. 2861-2866
    • Purwantini, E.1    Daniels, L.2
  • 362
    • 0031923498 scopus 로고    scopus 로고
    • 420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis
    • 420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis. J. Bacteriol. 180:2212-2219.
    • (1998) J. Bacteriol. , vol.180 , pp. 2212-2219
    • Purwantini, E.1    Daniels, L.2
  • 363
    • 71349084956 scopus 로고    scopus 로고
    • Deficiency in frataxin homologue YFH1 in the yeast Pichia guilliermondii leads to missregulation of iron acquisition and riboflavin biosynthesis and
    • Pynyaha, Y. V., et al. 2009. Deficiency in frataxin homologue YFH1 in the yeast Pichia guilliermondii leads to missregulation of iron acquisition and riboflavin biosynthesis and affects sulfate assimilation. Biometals 22:1051-1061.
    • (2009) Biometals , vol.22 , pp. 1051-1061
    • Pynyaha, Y.V.1
  • 364
    • 33644864128 scopus 로고    scopus 로고
    • Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: Stereochemical implications
    • Ramsperger, A., et al. 2006. Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: stereochemical implications. J. Biol. Chem. 281:1224-1232.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1224-1232
    • Ramsperger, A.1
  • 365
    • 0015163448 scopus 로고
    • Nucleotidases in plants. V. Purification & properties of an enzyme hydrolysing flavin adenine dinucleotide at acid pH value from Phaseolus radiatus
    • Ravindranath, S. D., and N. A. Rao. 1971. Nucleotidases in plants. V. Purification & properties of an enzyme hydrolysing flavin adenine dinucleotide at acid pH value from Phaseolus radiatus. Indian J. Biochem. 8:219-226.
    • (1971) Indian J. Biochem. , vol.8 , pp. 219-226
    • Ravindranath, S.D.1    Rao, N.A.2
  • 366
    • 28844501008 scopus 로고    scopus 로고
    • 2) uptake in Saccharomyces cerevisiae
    • 2) uptake in Saccharomyces cerevisiae. J. Biol. Chem. 280:39809-39817.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39809-39817
    • Reihl, P.1    Stolz, J.2
  • 367
    • 27744517816 scopus 로고    scopus 로고
    • GTP cyclohydrolase II structure and mechanism
    • Ren, J., et al. 2005. GTP cyclohydrolase II structure and mechanism. J. Biol. Chem. 280:36912-36919.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36912-36919
    • Ren, J.1
  • 368
    • 0002449548 scopus 로고    scopus 로고
    • Biosynthesis of the 5,6-dimethylbenzimidazole moiety of cobalamin and of the other bases found in natural corrinoids
    • R. Banerjee (ed.), Wiley, New York, NY
    • 12. Wiley, New York, NY.
    • (1999) 12 , pp. 557-575
    • Renz, P.1
  • 369
    • 0003137784 scopus 로고    scopus 로고
    • 12
    • B. Kräutler, D. Arigoni, and B. T. Golding (ed.), Wiley-VCH, Weinheim, Germany
    • 12 proteins. Wiley-VCH, Weinheim, Germany.
    • (2007) 12 Proteins , pp. 119-130
    • Renz, P.1
  • 371
    • 0019359295 scopus 로고
    • Biochemical and genetic characterisation of Streptomyces rimosus mutants impaired in oxytetracycline biosynthesis
    • Rhodes, P. M., N. Winskill, E. J. Friend, and M. Warren. 1981. Biochemical and genetic characterisation of Streptomyces rimosus mutants impaired in oxytetracycline biosynthesis. J. Gen. Microbiol. 124:329-338.
    • (1981) J. Gen. Microbiol. , vol.124 , pp. 329-338
    • Rhodes, P.M.1    Winskill, N.2    Friend, E.J.3    Warren, M.4
  • 372
    • 0026642218 scopus 로고
    • Biosynthesis of riboflavin: Cloning, sequencing, and expression of the gene coding for 3,4-dihydroxy-2-butanone 4-phosphate synthase of Escherichia coli
    • Richter, G., et al. 1992. Biosynthesis of riboflavin: cloning, sequencing, and expression of the gene coding for 3,4-dihydroxy-2-butanone 4-phosphate synthase of Escherichia coli. J. Bacteriol. 174:4050-4056.
    • (1992) J. Bacteriol. , vol.174 , pp. 4050-4056
    • Richter, G.1
  • 375
    • 0035933757 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: Studies on the mechanism of GTP cyclohydrolase II
    • Ritz, H., et al. 2001. Biosynthesis of riboflavin: studies on the mechanism of GTP cyclohydrolase II. J. Biol. Chem. 276:22273-22277.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22273-22277
    • Ritz, H.1
  • 376
    • 0003534929 scopus 로고
    • Plenum Press, New York, NY
    • Rivlin, R. S. (ed.). 1975. Riboflavin. Plenum Press, New York, NY.
    • (1975) Riboflavin
    • Rivlin, R.S.1
  • 377
    • 1542571790 scopus 로고    scopus 로고
    • A self-sufficient cytochrome P450 with a primary structural organization that includes a flavin domain and a [2Fe-2S] redox center
    • Roberts, G. A., et al. 2003. A self-sufficient cytochrome P450 with a primary structural organization that includes a flavin domain and a [2Fe-2S] redox center. J. Biol. Chem. 278:48914-48920.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48914-48920
    • Roberts, G.A.1
  • 378
    • 58149490653 scopus 로고    scopus 로고
    • A novel class of modular transporters for vitamins in prokaryotes
    • Rodionov, D. A., et al. 2009. A novel class of modular transporters for vitamins in prokaryotes. J. Bacteriol. 191:42-51.
    • (2009) J. Bacteriol. , vol.191 , pp. 42-51
    • Rodionov, D.A.1
  • 379
    • 49349089962 scopus 로고    scopus 로고
    • 2,5-Diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate synthases of fungi and archaea
    • Römisch-Margl, W., W. Eisenreich, I. Haase, A. Bacher, and M. Fischer. 2008. 2,5-Diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate synthases of fungi and archaea. FEBS J. 275:4403-4414.
    • (2008) FEBS J. , vol.275 , pp. 4403-4414
    • Römisch-Margl, W.1    Eisenreich, W.2    Haase, I.3    Bacher, A.4    Fischer, M.5
  • 380
    • 67650713931 scopus 로고    scopus 로고
    • The structural and functional diversity of metabolite-binding riboswitches
    • Roth, A., and R. R. Breaker. 2009. The structural and functional diversity of metabolite-binding riboswitches. Annu. Rev. Biochem. 78:305-334.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 305-334
    • Roth, A.1    Breaker, R.R.2
  • 381
    • 0025327227 scopus 로고
    • Qualitative and quantitative assessment of flavins in cow's milk
    • Roughead, Z. K., and D. B. McCormick. 1990. Qualitative and quantitative assessment of flavins in cow's milk. J. Nutr. 120:382-388.
    • (1990) J. Nutr. , vol.120 , pp. 382-388
    • Roughead, Z.K.1    McCormick, D.B.2
  • 382
    • 0014240337 scopus 로고
    • The biosynthesis of pteridines. V. The synthesis of riboflavin from pteridine precursors
    • Rowan, T., and H. C. Wood. 1968. The biosynthesis of pteridines. V. The synthesis of riboflavin from pteridine precursors. J. Chem. Soc. Perkin 1 4:452-458.
    • (1968) J. Chem. Soc. Perkin 1 , vol.4 , pp. 452-458
    • Rowan, T.1    Wood, H.C.2
  • 383
    • 77449158899 scopus 로고    scopus 로고
    • Dynamic flux responses in riboflavin overproducing Bacillus subtilis to increasing glucose limitation in fed-batch culture
    • Rühl, M., N. Zamboni, and U. Sauer. 2010. Dynamic flux responses in riboflavin overproducing Bacillus subtilis to increasing glucose limitation in fed-batch culture. Biotechnol. Bioeng. 105:795-804.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 795-804
    • Rühl, M.1    Zamboni, N.2    Sauer, U.3
  • 384
    • 0026032888 scopus 로고
    • Transport of riboflavin in human intestinal brush border membrane vesicles
    • Said, H. M., and P. Arianas. 1991. Transport of riboflavin in human intestinal brush border membrane vesicles. Gastroenterology 100:82-88.
    • (1991) Gastroenterology , vol.100 , pp. 82-88
    • Said, H.M.1    Arianas, P.2
  • 385
    • 0015851304 scopus 로고
    • Selection of microorganism producing flavin-adenine dinucleotide from FMN and adenine (AMP) and production of flavin-adenine dinucleotide by Sarcina lutea
    • Sakai, T., T. Watanabe, and I. Chibata. 1973. Selection of microorganism producing flavin-adenine dinucleotide from FMN and adenine (AMP) and production of flavin-adenine dinucleotide by Sarcina lutea. Agric. Biol. Chem. 37:849-856.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 849-856
    • Sakai, T.1    Watanabe, T.2    Chibata, I.3
  • 386
    • 0033786852 scopus 로고    scopus 로고
    • Cryptochrome: The second photoactive pigment in the eye and its role in circadian photoreception
    • Sancar, A. 2000. Cryptochrome: the second photoactive pigment in the eye and its role in circadian photoreception. Annu. Rev. Biochem. 69:31-67.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 31-67
    • Sancar, A.1
  • 387
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • Sancar, A. 2003. Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors. Chem. Rev. 103:2203-2237.
    • (2003) Chem. Rev. , vol.103 , pp. 2203-2237
    • Sancar, A.1
  • 388
    • 10044228602 scopus 로고    scopus 로고
    • Photolyase and cryptochrome blue-light photoreceptors
    • Sancar, A. 2004. Photolyase and cryptochrome blue-light photoreceptors. Adv. Protein Chem. 69:73-100.
    • (2004) Adv. Protein Chem. , vol.69 , pp. 73-100
    • Sancar, A.1
  • 389
    • 33644695717 scopus 로고    scopus 로고
    • An FMN hydrolase is fused to a riboflavin kinase homolog in plants
    • Sandoval, F. J., and S. Roje. 2005. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280:38337-38345.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38337-38345
    • Sandoval, F.J.1    Roje, S.2
  • 390
    • 57649221153 scopus 로고    scopus 로고
    • Flavin nucleotide metabolism in plants: Monofunctional enzymes synthesize FAD in plastids
    • Sandoval, F. Y., Y. Zhang, and S. Roje. 2008. Flavin nucleotide metabolism in plants: monofunctional enzymes synthesize FAD in plastids. J. Biol. Chem. 283:30890-30900.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30890-30900
    • Sandoval, F.Y.1    Zhang, Y.2    Roje, S.3
  • 391
    • 0028893491 scopus 로고
    • Riboflavin biosynthesis in Saccharomyces cerevisiae. Cloning, characterization, and expression of the RIB5 gene encoding riboflavin synthase
    • Santos, M. A., J. J. García-Ramírez, and J. L. Revuelta. 1995. Riboflavin biosynthesis in Saccharomyces cerevisiae. Cloning, characterization, and expression of the RIB5 gene encoding riboflavin synthase. J. Biol. Chem. 270:437-444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 437-444
    • Santos, M.A.1    García-Ramírez, J.J.2    Revuelta, J.L.3
  • 392
    • 0034666350 scopus 로고    scopus 로고
    • Molecular characterization of FMN1, the structural gene for the monofunctional flavokinase of Saccharomyces cerevisiae
    • Santos, M. A., A. Jimenez, and J. L. Revuelta. 2000. Molecular characterization of FMN1, the structural gene for the monofunctional flavokinase of Saccharomyces cerevisiae. J. Biol. Chem. 275:28618-28624.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28618-28624
    • Santos, M.A.1    Jimenez, A.2    Revuelta, J.L.3
  • 393
    • 33746046489 scopus 로고    scopus 로고
    • 2 producer fungus Ashbya gossypii
    • J. L. Barredo (ed.), Microbial processes and products. Humana Press Inc., Totowa, NJ
    • 2 producer fungus Ashbya gossypii, p. 283-300. In J. L. Barredo (ed.), Methods in biotechnology, vol. 18. Microbial processes and products. Humana Press Inc., Totowa, NJ.
    • (2006) Methods in Biotechnology , vol.18 , pp. 283-300
    • Santos, M.A.1    Mateos, L.2    Stahmann, K.P.3    Revuelta, J.L.4
  • 394
    • 6344272773 scopus 로고    scopus 로고
    • Candida albicans lacking the frataxin homologue: A relevant yeast model for studying the role of frataxin
    • Santos, R., et al. 2004. Candida albicans lacking the frataxin homologue: a relevant yeast model for studying the role of frataxin. Mol. Microbiol. 54:507-519.
    • (2004) Mol. Microbiol. , vol.54 , pp. 507-519
    • Santos, R.1
  • 395
    • 73849130625 scopus 로고    scopus 로고
    • Crystal structures of the lumazine protein from Photobacterium kishitanii in complexes with the authentic chromophore, 6,7- dimethyl-8-(1′-D- ribityl) lumazine, and its analogues, riboflavin and flavin mononucleotide, at high resolution
    • Sato, Y., et al. 2010. Crystal structures of the lumazine protein from Photobacterium kishitanii in complexes with the authentic chromophore, 6,7- dimethyl-8-(1′-D-ribityl) lumazine, and its analogues, riboflavin and flavin mononucleotide, at high resolution. J. Bacteriol. 192:127-133.
    • (2010) J. Bacteriol. , vol.192 , pp. 127-133
    • Sato, Y.1
  • 396
    • 0032551605 scopus 로고    scopus 로고
    • Metabolic capacity of Bacillus subtilis for the production of purine nucleosides, riboflavin, and folic acid
    • Sauer, U., D. C. Cameron, and J. E. Bailey. 1998. Metabolic capacity of Bacillus subtilis for the production of purine nucleosides, riboflavin, and folic acid. Biotechnol. Bioeng. 59:227-238.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 227-238
    • Sauer, U.1    Cameron, D.C.2    Bailey, J.E.3
  • 397
    • 0023228531 scopus 로고
    • Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs
    • Saxild, H. H., and P. Nygaard. 1987. Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs. J. Bacteriol. 169:2977-2983. (Pubitemid 17106314)
    • (1987) Journal of Bacteriology , vol.169 , Issue.7 , pp. 2977-2983
    • Saxild, H.H.1    Nygaard, P.2
  • 398
    • 0035215761 scopus 로고    scopus 로고
    • Transcriptional regulation of 3,4-dihydroxy-2-butanone 4-phosphate synthase
    • Schlösser, T., G. Schmidt, and K. P. Stahmann. 2001. Transcriptional regulation of 3,4-dihydroxy-2-butanone 4-phosphate synthase. Microbiology 147:3377-3386.
    • (2001) Microbiology , vol.147 , pp. 3377-3386
    • Schlösser, T.1    Schmidt, G.2    Stahmann, K.P.3
  • 399
    • 34548027721 scopus 로고    scopus 로고
    • Growth stress triggers riboflavin overproduction in Ashbya gossypii
    • Schlösser, T., et al. 2007. Growth stress triggers riboflavin overproduction in Ashbya gossypii. Appl. Microbiol. Biotechnol. 76:569-578.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 569-578
    • Schlösser, T.1
  • 400
    • 0347298691 scopus 로고    scopus 로고
    • Disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine in Ashbya gossypii
    • DOI 10.1042/BJ20021224
    • Schlüpen, C., et al. 2003. Disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine in Ashbya gossypii. Biochem. J. 369:263-273. (Pubitemid 36174196)
    • (2003) Biochemical Journal , vol.369 , Issue.2 , pp. 263-273
    • Schlupen, C.1    Santos, M.A.2    Weber, U.3    De Graaf, A.4    Revuelta, J.L.5    Stahmann, K.-P.6
  • 401
    • 0030042409 scopus 로고    scopus 로고
    • Correlation of isocitrate lyase activity and riboflavin formation in the riboflavin overproducer Ashbya gossypii
    • Schmidt, G., K. P. Stahmann, B. Kaesler, and H. Sahm. 1996. Correlation of isocitrate lyase activity and riboflavin formation in the riboflavin overproducer Ashbya gossypii. Microbiology 142:419-426. (Pubitemid 26068508)
    • (1996) Microbiology , vol.142 , Issue.2 , pp. 419-426
    • Schmidt, G.1    Stahmann, K.-P.2    Kaesler, B.3    Sahm, H.4
  • 402
    • 0030063010 scopus 로고    scopus 로고
    • Inhibition of purified isocitrate lyase identified itaconate and oxalate as potential antimetabolites for the riboflavin overproducer Ashbya gossypii
    • Schmidt, G., K. P. Stahmann, and H. Sahm. 1996. Inhibition of purified isocitrate lyase identified itaconate and oxalate as potential antimetabolites for the riboflavin overproducer Ashbya gossypii. Microbiology 142:411-417. (Pubitemid 26068289)
    • (1996) Microbiology , vol.142 , Issue.2 , pp. 411-417
    • Schmidt, G.1    Stahmann, K.-P.2    Sahm, H.3
  • 403
    • 0025254080 scopus 로고
    • Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit
    • Schott, K., J. Kellermann, F. Lottspeich, and A. Bacher. 1990. Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit. J. Biol. Chem. 265:4204-4209.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4204-4209
    • Schott, K.1    Kellermann, J.2    Lottspeich, F.3    Bacher, A.4
  • 404
    • 0035941188 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
    • Schramek, N., A. Bracher, and A. Bacher. 2001. Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II. J. Biol. Chem. 276:44157-44162.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44157-44162
    • Schramek, N.1    Bracher, A.2    Bacher, A.3
  • 405
    • 0008024857 scopus 로고
    • Reversible enzymatic synthesis of flavin-adenine dinucleotide
    • Schrecker, A. W., and A. Kornberg. 1950. Reversible enzymatic synthesis of flavin-adenine dinucleotide. J. Biol. Chem. 182:795-803.
    • (1950) J. Biol. Chem. , vol.182 , pp. 795-803
    • Schrecker, A.W.1    Kornberg, A.2
  • 406
    • 62249156218 scopus 로고    scopus 로고
    • Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch
    • Serganov, A., L. Huang, and D. J. Patel. 2009. Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch. Nature 458:233-237.
    • (2009) Nature , vol.458 , pp. 233-237
    • Serganov, A.1    Huang, L.2    Patel, D.J.3
  • 407
    • 34548778155 scopus 로고    scopus 로고
    • Ribozymes, riboswitches and beyond: Regulation of gene expression without proteins
    • Serganov, A., and D. J. Patel. 2007. Ribozymes, riboswitches and beyond: regulation of gene expression without proteins. Nat. Rev. Genet. 8:776-790.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 776-790
    • Serganov, A.1    Patel, D.J.2
  • 408
    • 39149119601 scopus 로고    scopus 로고
    • Towards deciphering the principles underlying an mRNA recognition code
    • Serganov, A., and D. J. Patel. 2008. Towards deciphering the principles underlying an mRNA recognition code. Curr. Opin. Struct. Biol. 18:120-129.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 120-129
    • Serganov, A.1    Patel, D.J.2
  • 409
    • 0022034731 scopus 로고
    • Genetic control of riboflavin biosynthesis in Pichia guilliermondii yeasts. The detection of a new regulator gene RIB81
    • Shavlovskii, G. M., L. I. Babiak, A. A. Sibirnyi, and E. M. Logvinenko. 1985. Genetic control of riboflavin biosynthesis in Pichia guilliermondii yeasts. The detection of a new regulator gene RIB81. Genetika 21:368-374.
    • (1985) Genetika , vol.21 , pp. 368-374
    • Shavlovskii, G.M.1    Babiak, L.I.2    Sibirnyi, A.A.3    Logvinenko, E.M.4
  • 410
    • 0017624764 scopus 로고
    • The activity of enzymes involved in synthesis and hydrolysis of flavin adenine dinucleotide in Pichia guilliermondii: Studies at different levels of flavinogenesis
    • In Russian
    • Shavlovskii, G. M., and D. V. Fedorovich. 1977. The activity of enzymes involved in synthesis and hydrolysis of flavin adenine dinucleotide in Pichia guilliermondii: studies at different levels of flavinogenesis. Mikrobiologiia 46:904-911. (In Russian.)
    • (1977) Mikrobiologiia , vol.46 , pp. 904-911
    • Shavlovskii, G.M.1    Fedorovich, D.V.2
  • 411
    • 0013636798 scopus 로고
    • Effects of rib81 mutation on riboflavin biosynthesis and iron transport in the yeast Pichia guilliermondii
    • In Russian
    • Shavlovskii, G. M., Fedorovich, and L. Y. Babiak. 1993. Effects of rib81 mutation on riboflavin biosynthesis and iron transport in the yeast Pichia guilliermondii. Mikrobiologiia 62:897-904. (In Russian.)
    • (1993) Mikrobiologiia , vol.62 , pp. 897-904
    • Shavlovskii, G.M.1    Fedorovich2    Babiak, L.Y.3
  • 412
    • 0026455051 scopus 로고
    • Involvement of gene RIB80 in regulation of riboflavin biosynthesis and iron transport in Pichia guilliermondii
    • In Russian
    • Shavlovskii, G. M., D. V. Fedorovich, V. I. Kutsiaba, L. Y. Babiak, and N. N. Stenchuk. 1992. Involvement of gene RIB80 in regulation of riboflavin biosynthesis and iron transport in Pichia guilliermondii. Genetika 28:25-32. (In Russian.)
    • (1992) Genetika , vol.28 , pp. 25-32
    • Shavlovskii, G.M.1    Fedorovich, D.V.2    Kutsiaba, V.I.3    Babiak, L.Y.4    Stenchuk, N.N.5
  • 413
    • 0022392763 scopus 로고
    • Isolation and characterization of the flavinogenic strains of Pichia guilliermondii bearing regulatory mutation rib80 (ribR)
    • In Russian
    • Shavlovskii, G. M., D. V. Fedorovich, E. M. Logvinenko, and L. V. Koltun. 1985. Isolation and characterization of the flavinogenic strains of Pichia guilliermondii bearing regulatory mutation rib80 (ribR). Mikrobiologiia 54:919-925. (In Russian.)
    • (1985) Mikrobiologiia , vol.54 , pp. 919-925
    • Shavlovskii, G.M.1    Fedorovich, D.V.2    Logvinenko, E.M.3    Koltun, L.V.4
  • 414
    • 0018039593 scopus 로고
    • Regulation of the activity of GTP-cyclohydrolase, the enzyme of the first step of flavinogenesis in yeasts
    • In Russian
    • Shavlovskii, G. M., L. V. Koltun, and V. E. Kashchenko. 1978. Regulation of the activity of GTP-cyclohydrolase, the enzyme of the first step of flavinogenesis in yeasts. Biokhimiia 43:2074-2081. (In Russian.)
    • (1978) Biokhimiia , vol.43 , pp. 2074-2081
    • Shavlovskii, G.M.1    Koltun, L.V.2    Kashchenko, V.E.3
  • 415
    • 0039420276 scopus 로고
    • Regulation of biosynthesis of riboflavin by elements of positive control in Pichia guilliermondii yeast
    • In Russian
    • Shavlovskii, G. M., L. V. Koltun, B. V. Kshanovskaya, E. M. Logvinenko, and N. N. Stenchuk. 1989. Regulation of biosynthesis of riboflavin by elements of positive control in Pichia guilliermondii yeast. Genetika 25:250-258. (In Russian.)
    • (1989) Genetika , vol.25 , pp. 250-258
    • Shavlovskii, G.M.1    Koltun, L.V.2    Kshanovskaya, B.V.3    Logvinenko, E.M.4    Stenchuk, N.N.5
  • 417
    • 0024041684 scopus 로고
    • Supersynthesis of flavins in microorganisms and its molecular mechanism (review of the literature)
    • In Russian
    • Shavlovskii, G. M., and E. M. Logvinenko. 1988. Supersynthesis of flavins in microorganisms and its molecular mechanism (review of the literature). Prikl. Biokhim Mikrobiol. 24:435-447. (In Russian.)
    • (1988) Prikl. Biokhim Mikrobiol. , vol.24 , pp. 435-447
    • Shavlovskii, G.M.1    Logvinenko, E.M.2
  • 418
    • 17444441446 scopus 로고
    • Detection in Pichia guilliermondii of GTP-cyclohydrolase, an enzyme involved in the 1st stage of flavinogenesis
    • In Russian
    • Shavlovskii, G. M., E. M. Logvinenko, V. E. Kashchenko, L. V. Koltun, and A. E. Zakalskii. 1976. Detection in Pichia guilliermondii of GTP-cyclohydrolase, an enzyme involved in the 1st stage of flavinogenesis. Dokl. Akad. Nauk SSSR 230:1485-1487. (In Russian.)
    • (1976) Dokl. Akad. Nauk SSSR , vol.230 , pp. 1485-1487
    • Shavlovskii, G.M.1    Logvinenko, E.M.2    Kashchenko, V.E.3    Koltun, L.V.4    Zakalskii, A.E.5
  • 419
    • 0019643055 scopus 로고
    • Activity of the enzyme of the 2d step of flavinogen-esis, 2,5-diamino-6-hydroxy-4-ribosylaminopyrimidine-5′-phosphate reductase, in Pichia guilliermondii yeasts
    • In Russian
    • Shavlovskii, G. M., E. M. Logvinenko, A. A. Sibirnyi, D. V. Fedorovich, and A. E. Zakalskii. 1981. Activity of the enzyme of the 2d step of flavinogen-esis, 2,5-diamino-6-hydroxy-4-ribosylaminopyrimidine-5′- phosphate reductase, in Pichia guilliermondii yeasts. Mikrobiologiia 50:1008-1011. (In Russian.)
    • (1981) Mikrobiologiia , vol.50 , pp. 1008-1011
    • Shavlovskii, G.M.1    Logvinenko, E.M.2    Sibirnyi, A.A.3    Fedorovich, D.V.4    Zakalskii, A.E.5
  • 420
    • 0020755219 scopus 로고
    • Purification and some properties of GTP cyclohydrolase of the yeast Pichia guilliermondii
    • In Russian
    • Shavlovskii, G. M., E. M. Logvinenko, and A. E. Zakalskii. 1983. Purification and some properties of GTP cyclohydrolase of the yeast Pichia guilliermondii. Biokhimia 48:837-843. (In Russian.)
    • (1983) Biokhimia , vol.48 , pp. 837-843
    • Shavlovskii, G.M.1    Logvinenko, E.M.2    Zakalskii, A.E.3
  • 421
    • 0020039454 scopus 로고
    • Selection and mutant properties of Pichia guilliermondii yeasts with derepressed GTP cyclohydrolase, the enzyme of the 1st step in flavinogenesis
    • In Russian
    • Shavlovskii, G. M., A. A. Sibirnyi, D. V. Fedorovich, and E. Z. Seniuta. 1982. Selection and mutant properties of Pichia guilliermondii yeasts with derepressed GTP cyclohydrolase, the enzyme of the 1st step in flavinogenesis. Mikrobiologiia 51:96-101. (In Russian.)
    • (1982) Mikrobiologiia , vol.51 , pp. 96-101
    • Shavlovskii, G.M.1    Sibirnyi, A.A.2    Fedorovich, D.V.3    Seniuta, E.Z.4
  • 422
    • 0018521339 scopus 로고
    • Genetic classification of riboflavin-dependent mutants of Pichia guilliermondii yeasts
    • In Russian
    • Shavlovskii, G. M., A. A. Sibirnyi, B. V. Kshanovskaia, L. V. Koltun, and E. M. Logvinenko. 1979. Genetic classification of riboflavin-dependent mutants of Pichia guilliermondii yeasts. Genetika 15:1561-1568. (In Russian.)
    • (1979) Genetika , vol.15 , pp. 1561-1568
    • Shavlovskii, G.M.1    Sibirnyi, A.A.2    Kshanovskaia, B.V.3    Koltun, L.V.4    Logvinenko, E.M.5
  • 423
    • 0019122938 scopus 로고
    • Overproduction of riboflavin in mutants of Pichia guilliermondii yeasts resistant to 7-methyl-8-trifluoromethyl-10-(1′-D-ribityl)isoalloxazine
    • In Russian
    • Shavlovskii, G. M., A. A. Sibirnyi, G. P. Ksheminskaya, and G. E. Pinchuk. 1980. Overproduction of riboflavin in mutants of Pichia guilliermondii yeasts resistant to 7-methyl-8-trifluoromethyl-10-(1′-D-ribityl) isoalloxazine. Mikrobiologiia 49:702-707. (In Russian.)
    • (1980) Mikrobiologiia , vol.49 , pp. 702-707
    • Shavlovskii, G.M.1    Sibirnyi, A.A.2    Ksheminskaya, G.P.3    Pinchuk, G.E.4
  • 424
    • 0020214783 scopus 로고
    • Flavinogenesis regulation in riboflavin-dependent Escherichia coli mutants
    • In Russian
    • Shavlovskii, G. M., G. E. Tesliar, and L. P. Strugovshchikova. 1982. Flavinogenesis regulation in riboflavin-dependent Escherichia coli mutants. Mikrobiologiia 51:986-992. (In Russian.)
    • (1982) Mikrobiologiia , vol.51 , pp. 986-992
    • Shavlovskii, G.M.1    Tesliar, G.E.2    Strugovshchikova, L.P.3
  • 425
    • 0017871041 scopus 로고
    • Flavinogenic activity of natural strains of the yeast Pichia guilliermondii
    • In Russian
    • Shavlovskii, G. M., et al. 1978. Flavinogenic activity of natural strains of the yeast Pichia guilliermondii. Prikl. Biokhim. Mikrobiol. 14:184-189. (In Russian.)
    • (1978) Prikl. Biokhim. Mikrobiol. , vol.14 , pp. 184-189
    • Shavlovskii, G.M.1
  • 426
    • 0016527696 scopus 로고
    • Determination of riboflavin kinase activity in yeast
    • In Ukrainian
    • Shavlovsky, G. M., and V. E. Kashchenko. 1975. Determination of riboflavin kinase activity in yeast. Ukr. Biokhim. Zh. 47:536-541. (In Ukrainian.)
    • (1975) Ukr. Biokhim. Zh. , vol.47 , pp. 536-541
    • Shavlovsky, G.M.1    Kashchenko, V.E.2
  • 427
    • 0018962039 scopus 로고
    • First reaction of riboflavin biosynthesis: Catalysis by a guanosine triphosphate cyclohydrolase from yeast
    • Schavlovsky, G. M., et al. 1980. First reaction of riboflavin biosynthesis: catalysis by a guanosine triphosphate cyclohydrolase from yeast. Arch. Microbiol. 124:255-259.
    • (1980) Arch. Microbiol. , vol.124 , pp. 255-259
    • Schavlovsky, G.M.1
  • 428
    • 22244471311 scopus 로고
    • Riboflavin transport in yeasts and its regulation
    • I. S. Kulaev, D. W. Tempest, and E. A. Dawes (ed.), Academic Press, London, United Kingdom
    • Shavlovsky, G. M., and A. A. Sibirny. 1985. Riboflavin transport in yeasts and its regulation, p. 385-392. In I. S. Kulaev, D. W. Tempest, and E. A. Dawes (ed.), Environmental regulation of microbial metabolism. Academic Press, London, United Kingdom.
    • (1985) Environmental Regulation of Microbial Metabolism , pp. 385-392
    • Shavlovsky, G.M.1    Sibirny, A.A.2
  • 429
    • 79958061115 scopus 로고
    • Permease and "excretase" for riboflavin in the mutants of Pichia guilliermondii yeast
    • Shavlovsky, G. M., A. A. Sibirny, and G. P. Ksheminskaya. 1977. Permease and "excretase" for riboflavin in the mutants of Pichia guilliermondii yeast. Biochem. Physiol. Pflanzen. 171:139-145.
    • (1977) Biochem. Physiol. Pflanzen. , vol.171 , pp. 139-145
    • Shavlovsky, G.M.1    Sibirny, A.A.2    Ksheminskaya, G.P.3
  • 431
    • 68049129551 scopus 로고    scopus 로고
    • Transcriptome analysis guided metabolic engineering of Bacillus subtilis for riboflavin production
    • Shi, S., T. Chen, Z. Zhang, X. Chen, and X. Zhao. 2009. Transcriptome analysis guided metabolic engineering of Bacillus subtilis for riboflavin production. Metab. Eng. 11:243-252.
    • (2009) Metab. Eng. , vol.11 , pp. 243-252
    • Shi, S.1    Chen, T.2    Zhang, Z.3    Chen, X.4    Zhao, X.5
  • 432
    • 34249871205 scopus 로고    scopus 로고
    • Vitamins and related compounds: Microbial production
    • H. Rehm (ed)., Wiley-VCH, Weinheim, Germany
    • Shimizu, S. 2001. Vitamins and related compounds: microbial production, p. 322-326. In H. Rehm (ed)., Biotechnology, vol. 10. Wiley-VCH, Weinheim, Germany.
    • (2001) Biotechnology , vol.10 , pp. 322-326
    • Shimizu, S.1
  • 433
    • 0017730529 scopus 로고
    • Derepression of FAD pyrophosphorylase and flavin changes during growth of Kloeckera sp. no. 2201 on methanol
    • Shimizu, S., M. Ishida, N. Kato, Y. Tani, and K. Ogata. 1977. Derepression of FAD pyrophosphorylase and flavin changes during growth of Kloeckera sp. no. 2201 on methanol. Agric. Biol. Chem. 41:2215-2220.
    • (1977) Agric. Biol. Chem. , vol.41 , pp. 2215-2220
    • Shimizu, S.1    Ishida, M.2    Kato, N.3    Tani, Y.4    Ogata, K.5
  • 434
    • 0017379686 scopus 로고
    • Flavin changes of Kloeckera sp. no. 2201 during adaptation to methanol
    • Shimizu, S., M. Ishida, Y. Tani, and K. Ogata. 1977. Flavin changes of Kloeckera sp. no. 2201 during adaptation to methanol. Agric. Biol. Chem. 41:423-424.
    • (1977) Agric. Biol. Chem. , vol.41 , pp. 423-424
    • Shimizu, S.1    Ishida, M.2    Tani, Y.3    Ogata, K.4
  • 436
    • 0022607709 scopus 로고
    • Coenzyme models. 40. Spectral and reactivity studies of roseoflavin analogs: Correlation between reactivity and spectral parameters
    • Shinkai, S., et al. 1986. Coenzyme models. 40. Spectral and reactivity studies of roseoflavin analogs: correlation between reactivity and spectral parameters. Bioorg. Chem. 14:119-133.
    • (1986) Bioorg. Chem. , vol.14 , pp. 119-133
    • Shinkai, S.1
  • 437
    • 79958044536 scopus 로고
    • Studies on the production of riboflavin by Aspergillus niger
    • Shukla, J. P., and K. A. Prabku. 1961. Studies on the production of riboflavin by Aspergillus niger. J. Sci. Ind. Res. 40:20-24.
    • (1961) J. Sci. Ind. Res. , vol.40 , pp. 20-24
    • Shukla, J.P.1    Prabku, K.A.2
  • 438
    • 19544382381 scopus 로고    scopus 로고
    • Pichia guilliermondii
    • K. Wolf (ed.), Springer Verlag, Berlin, Germany
    • Sibirny, A. A. 1996. Pichia guilliermondii, p. 255-272. In K. Wolf (ed.), Nonconventional yeasts in biotechnology. Springer Verlag, Berlin, Germany.
    • (1996) Nonconventional Yeasts in Biotechnology , pp. 255-272
    • Sibirny, A.A.1
  • 439
    • 79251608940 scopus 로고    scopus 로고
    • Pichia guilliermondii
    • T. Satyanarayana and G. Kunze (ed.), Springer Science, New York, NY
    • Sibirny, A. A., and Y. R. Boretsky. 2009. Pichia guilliermondii, p. 113-134. In T. Satyanarayana and G. Kunze (ed.), Yeast biotechnology: diversity and applications. Springer Science, New York, NY.
    • (2009) Yeast Biotechnology: Diversity and Applications , pp. 113-134
    • Sibirny, A.A.1    Boretsky, Y.R.2
  • 441
    • 79958040321 scopus 로고    scopus 로고
    • The yeast strain Candida famata IMB Y-5034, the riboflavin producer
    • May UA patent no. 90754
    • Sibirny, A. A., K. V. Dmytruk, and D. V. Fedorovych. May 2010. The yeast strain Candida famata IMB Y-5034, the riboflavin producer. UA patent no. 90754.
    • (2010)
    • Sibirny, A.A.1    Dmytruk, K.V.2    Fedorovych, D.V.3
  • 442
    • 0021348430 scopus 로고
    • Identification of regulatory genes of riboflavin permease and α-glucosidase in the yeast Pichia guilliermondii
    • Sibirny, A. A., and G. M. Shavlovsky. 1984. Identification of regulatory genes of riboflavin permease and α-glucosidase in the yeast Pichia guilliermondii. Curr. Genet. 8:107-114.
    • (1984) Curr. Genet. , vol.8 , pp. 107-114
    • Sibirny, A.A.1    Shavlovsky, G.M.2
  • 443
    • 79958035397 scopus 로고    scopus 로고
    • Candida famata (Debaryomyces hansenii)
    • T. Satyanarayana and G. Kunze (ed.), Springer Science, New York, NY
    • Sibirny, A. A., and A. Y. Voronovsky. 2009. Candida famata (Debaryomyces hansenii), p. 85-111. In T. Satyanarayana and G. Kunze (ed.), Yeast biotechnology: diversity and applications. Springer Science, New York, NY.
    • (2009) Yeast Biotechnology: Diversity and Applications , pp. 85-111
    • Sibirny, A.A.1    Voronovsky, A.Y.2
  • 444
    • 0019631547 scopus 로고
    • Riboflavin transport in the mutant of Pichia guilliermondii yeast defective in glucose uptake
    • In Russian
    • Sibirnyi, A. A., G. P. Ksheminskaya, A. G. Orlovskaya, and G. M. Shavlovskii. 1981. Riboflavin transport in the mutant of Pichia guilliermondii yeast defective in glucose uptake. Biokhimiia 46:1761-1763. (In Russian.)
    • (1981) Biokhimiia , vol.46 , pp. 1761-1763
    • Sibirnyi, A.A.1    Ksheminskaya, G.P.2    Orlovskaya, A.G.3    Shavlovskii, G.M.4
  • 445
    • 0017941428 scopus 로고
    • On the inhibition of alkaline phosphatase I of the yeast Pichia guilliermondii in vitro and in vivo
    • In Russian
    • Sibirnyi, A. A., and G. M. Shavlovskii. 1978. On the inhibition of alkaline phosphatase I of the yeast Pichia guilliermondii in vitro and in vivo. Ukr. Biokhim. Zhurn. 50:226-231. (In Russian.)
    • (1978) Ukr. Biokhim. Zhurn. , vol.50 , pp. 226-231
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2
  • 446
    • 0019546951 scopus 로고
    • Increase in yeast and bacterial sensitivity to inhibitors and riboflavin as affected by high sulfate and phosphate concentrations
    • In Russian
    • Sibirnyi, A. A., and G. M. Shavlovskii. 1981. Increase in yeast and bacterial sensitivity to inhibitors and riboflavin as affected by high sulfate and phosphate concentrations. Mikrobiologiia 50:242-248. (In Russian.)
    • (1981) Mikrobiologiia , vol.50 , pp. 242-248
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2
  • 449
    • 0017685556 scopus 로고
    • The mutants of the yeast Pichia guilliermondii with multiple sensitivity to antibiotics and antimetabolites. Selection and some properties of the mutants
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, and G. V. Goloshchapova. 1977. The mutants of the yeast Pichia guilliermondii with multiple sensitivity to antibiotics and antimetabolites. Selection and some properties of the mutants. Genetika 13:872-879. (In Russian.)
    • (1977) Genetika , vol.13 , pp. 872-879
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Goloshchapova, G.V.3
  • 450
    • 0017603069 scopus 로고
    • Hybridization and meiotic segregation in the paraffin-utilizing yeast Pichia guilliermondii Wickerham
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, G. P. Ksheminskaya, and G. I. Naumov. 1977. Hybridization and meiotic segregation in the paraffin-utilizing yeast Pichia guilliermondii Wickerham. Genetika 13:314-321. (In Russian.)
    • (1977) Genetika , vol.13 , pp. 314-321
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Ksheminskaya, G.P.3    Naumov, G.I.4
  • 451
    • 0017625164 scopus 로고
    • Active riboflavin transport in the yeast Pichia guilliermondii. Finding and properties of the cryptic riboflavin permease
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, G. P. Ksheminskaya, and A. G. Orlovskaya. 1977. Active riboflavin transport in the yeast Pichia guilliermondii. Finding and properties of the cryptic riboflavin permease. Biokhimiia 42:1841-1851. (In Russian.)
    • (1977) Biokhimiia , vol.42 , pp. 1841-1851
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Ksheminskaya, G.P.3    Orlovskaya, A.G.4
  • 452
    • 0017462491 scopus 로고
    • On riboflavin transport in the cells of riboflavinless yeast mutants
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, G. P. Ksheminskaya, and A. G. Orlovskaya. 1977. On riboflavin transport in the cells of riboflavinless yeast mutants. Mikrobiologiia 46:376-378. (In Russian.)
    • (1977) Mikrobiologiia , vol.46 , pp. 376-378
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Ksheminskaya, G.P.3    Orlovskaya, A.G.4
  • 453
    • 0018195824 scopus 로고
    • The influence of glucose and some its derivates on the systems for uptake and excretion of riboflavin in yeast Pichia guilliermondii
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, G. P. Ksheminskaya, and A. G. Orlovskaya. 1978. The influence of glucose and some its derivates on the systems for uptake and excretion of riboflavin in yeast Pichia guilliermondii. Biokhimiia 43:1414-1422. (In Russian.)
    • (1978) Biokhimiia , vol.43 , pp. 1414-1422
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Ksheminskaya, G.P.3    Orlovskaya, A.G.4
  • 454
    • 0018511330 scopus 로고
    • Coordinate regulation of riboflavin permease and α-glucosidase synthesis in the yeast Pichia guilliermondii
    • In Russian
    • Sibirnyi, A. A., G. M. Shavlovskii, G. P. Ksheminskaya, and A. G. Orlovskaya. 1979. Coordinate regulation of riboflavin permease and α-glucosidase synthesis in the yeast Pichia guilliermondii. Biokhimiia 44:1558-1568. (In Russian.)
    • (1979) Biokhimiia , vol.44 , pp. 1558-1568
    • Sibirnyi, A.A.1    Shavlovskii, G.M.2    Ksheminskaya, G.P.3    Orlovskaya, A.G.4
  • 456
    • 0017514623 scopus 로고
    • Selection of a genetic strain of Pichia guilliermondii yeasts capable of forming a significant quantity of spores
    • In Russian
    • Sibirnyi, A. A., V. P. Zharova, B. V. Kshanovskaia, and G. M. Shavlovskii. 1977. Selection of a genetic strain of Pichia guilliermondii yeasts capable of forming a significant quantity of spores. Tsitol. Genet. 11:330-333. (In Russian.)
    • (1977) Tsitol. Genet. , vol.11 , pp. 330-333
    • Sibirnyi, A.A.1    Zharova, V.P.2    Kshanovskaia, B.V.3    Shavlovskii, G.M.4
  • 457
    • 0020403957 scopus 로고
    • Vitamin and nitrogen base requirements for Listeria monocytogenes and haemolysin production
    • Siddiqi, R., and M. A. Khan. 1982. Vitamin and nitrogen base requirements for Listeria monocytogenes and haemolysin production. Zentralbl. Bakteriol. Mikrobiol. Hyg. A. 253:225-235.
    • (1982) Zentralbl. Bakteriol. Mikrobiol. Hyg. A. , vol.253 , pp. 225-235
    • Siddiqi, R.1    Khan, M.A.2
  • 458
    • 13144254969 scopus 로고
    • A microbiological assay for riboflavin
    • Snell, E. E., and F. M. Strong. 1939. A microbiological assay for riboflavin. Ind. Eng. Chem. Anal. ed. 11:346-350.
    • (1939) Ind. Eng. Chem. Anal. Ed. , vol.11 , pp. 346-350
    • Snell, E.E.1    Strong, F.M.2
  • 459
    • 12844287079 scopus 로고    scopus 로고
    • The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
    • Solovieva, I. M., R. A. Kreneva, L. Errais Lopez, and D. A. Perumov. 2005. The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product. FEMS Microbiol. Lett. 243:51-58.
    • (2005) FEMS Microbiol. Lett. , vol.243 , pp. 51-58
    • Solovieva, I.M.1    Kreneva, R.A.2    Errais Lopez, L.3    Perumov, D.A.4
  • 460
    • 0032924988 scopus 로고    scopus 로고
    • The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of Bacillus subtilis riboflavin operon
    • Solovieva, I. M., R. A. Kreneva, D. J. Leak, and D. A. Perumov. 1999. The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of Bacillus subtilis riboflavin operon. Mikrobiologiia 145:67-73.
    • (1999) Mikrobiologiia , vol.145 , pp. 67-73
    • Solovieva, I.M.1    Kreneva, R.A.2    Leak, D.J.3    Perumov, D.A.4
  • 461
    • 0020080722 scopus 로고
    • Riboflavin transport by rabbit kidney slices: Characterization and relation to cyclic organic acid transport
    • Spector, R. 1982. Riboflavin transport by rabbit kidney slices: characterization and relation to cyclic organic acid transport. J. Pharmacol. Exp. Ther. 221:394-398.
    • (1982) J. Pharmacol. Exp. Ther. , vol.221 , pp. 394-398
    • Spector, R.1
  • 462
    • 61849165016 scopus 로고    scopus 로고
    • The proline-dependent transcription factor Put3 regulates the expression of the riboflavin transporter MCH5 in Saccharomyces cerevisiae
    • Spitzner, A., A. F. Perzlmaier, K. E. Geillinger, P. Reihl, and J. Stolz. 2008. The proline-dependent transcription factor Put3 regulates the expression of the riboflavin transporter MCH5 in Saccharomyces cerevisiae. Genetics 180: 2007-2017.
    • (2008) Genetics , vol.180 , pp. 2007-2017
    • Spitzner, A.1    Perzlmaier, A.F.2    Geillinger, K.E.3    Reihl, P.4    Stolz, J.5
  • 463
    • 33750706955 scopus 로고    scopus 로고
    • Evolution of new function in the GTP cyclohydrolase II proteins of Streptomyces coelicolor
    • Spoonamore, J. E., A. L. Dahlgran, N. E. Jacobsen, and V. Bandarian. 2006. Evolution of new function in the GTP cyclohydrolase II proteins of Streptomyces coelicolor. Biochemistry 45:12144-12155.
    • (2006) Biochemistry , vol.45 , pp. 12144-12155
    • Spoonamore, J.E.1    Dahlgran, A.L.2    Jacobsen, N.E.3    Bandarian, V.4
  • 464
    • 0034091478 scopus 로고    scopus 로고
    • Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production
    • Stahmann, K. P., J. L. Revuelta, and H. Seulberger. 2000. Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production. Appl. Microbiol. Biotechnol. 53:509-516.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 509-516
    • Stahmann, K.P.1    Revuelta, J.L.2    Seulberger, H.3
  • 465
    • 0035209716 scopus 로고    scopus 로고
    • Riboflavin, overproduced during sporulation of Ashbya gossypii, protects its hyaline spores against ultraviolet light
    • Stahmann, K. P., et al. 2001. Riboflavin, overproduced during sporulation of Ashbya gossypii, protects its hyaline spores against ultraviolet light. Environ. Microbiol. 3:545-550.
    • (2001) Environ. Microbiol. , vol.3 , pp. 545-550
    • Stahmann, K.P.1
  • 466
    • 1542319811 scopus 로고    scopus 로고
    • A hexose transporter homologue controls glucose repression in the methylotrophic yeast Hansenula polymorpha
    • Stasyk, O. V., et al. 2004. A hexose transporter homologue controls glucose repression in the methylotrophic yeast Hansenula polymorpha. J. Biol. Chem. 279:8116-8125.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8116-8125
    • Stasyk, O.V.1
  • 467
    • 3843091016 scopus 로고    scopus 로고
    • Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate
    • Steinbacher, S., S. Schiffmann, A. Bacher, and M. Fischer. 2004. Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate. Acta Crystallogr. D Biol. Crystallogr. 60:1338-1340.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1338-1340
    • Steinbacher, S.1    Schiffmann, S.2    Bacher, A.3    Fischer, M.4
  • 468
    • 0142242191 scopus 로고    scopus 로고
    • Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: Implications for the catalytic mechanism
    • Steinbacher, S., et al. 2003. Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism. J. Biol. Chem. 278:42256-42265.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42256-42265
    • Steinbacher, S.1
  • 469
    • 0027972417 scopus 로고
    • Sequence and promoter analysis of the highly expressed TEF gene of the filamentous fungus Ashbya gossypii
    • Steiner, S., and P. Philippsen. 1994. Sequence and promoter analysis of the highly expressed TEF gene of the filamentous fungus Ashbya gossypii. Mol. Gen. Genet. 242:263-271.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 263-271
    • Steiner, S.1    Philippsen, P.2
  • 470
    • 0029022709 scopus 로고
    • Homologous recombination as the main mechanism for DNA integration and cause of rearrangements in the filamentous ascomycete Ashbya gossypii
    • Steiner, S., J. Wendland, M. C. Wright, and P. Philippsen. 1995. Homologous recombination as the main mechanism for DNA integration and cause of rearrangements in the filamentous ascomycete Ashbya gossypii. Genetics 140:973-987.
    • (1995) Genetics , vol.140 , pp. 973-987
    • Steiner, S.1    Wendland, J.2    Wright, M.C.3    Philippsen, P.4
  • 471
    • 84891051011 scopus 로고    scopus 로고
    • The new gene RED1 controlling biosynthesis of riboflavin and ferrireductase activity in the yeast Pichia guilliermondii
    • In Ukrainian
    • Stenchuk, M. M., and K. E. Kapustyak. 1999. The new gene RED1 controlling biosynthesis of riboflavin and ferrireductase activity in the yeast Pichia guilliermondii. Biopolymers Cell 15:522-528. (In Ukrainian.)
    • (1999) Biopolymers Cell , vol.15 , pp. 522-528
    • Stenchuk, M.M.1    Kapustyak, K.E.2
  • 472
    • 0642371267 scopus 로고    scopus 로고
    • The red mutations impair regulation of flavinogenesis and metal homeostasis in the yeast Pichia guilliermondii
    • In Russian
    • Stenchuk, N. N., and K. E. Kapustyak. 2003. The red mutations impair regulation of flavinogenesis and metal homeostasis in the yeast Pichia guilliermondii. Genetika 39:1026-1032. (In Russian.)
    • (2003) Genetika , vol.39 , pp. 1026-1032
    • Stenchuk, N.N.1    Kapustyak, K.E.2
  • 473
    • 0035524972 scopus 로고    scopus 로고
    • Effect of rib83 mutation on riboflavin biosynthesis and iron assimilation in Pichia guilliermondii
    • In Russian
    • Stenchuk, N. N., V. I. Kutsiaba, B. V. Kshanovskaia, and D. V. Fedorovich. 2001. Effect of rib83 mutation on riboflavin biosynthesis and iron assimilation in Pichia guilliermondii. Mikrobiologiia 70:753-758. (In Russian.)
    • (2001) Mikrobiologiia , vol.70 , pp. 753-758
    • Stenchuk, N.N.1    Kutsiaba, V.I.2    Kshanovskaia, B.V.3    Fedorovich, D.V.4
  • 474
    • 0025845027 scopus 로고
    • The mutants of Pichia guilliermondii with enhanced ability to reduce iron ions and riboflavin
    • In Russian
    • Stenchuk, N. N., O. V. Protchenko, D. V. Fedorovich, and G. M. Shavlovskii. 1991. The mutants of Pichia guilliermondii with enhanced ability to reduce iron ions and riboflavin. Genetika 27:561-564. (In Russian.)
    • (1991) Genetika , vol.27 , pp. 561-564
    • Stenchuk, N.N.1    Protchenko, O.V.2    Fedorovich, D.V.3    Shavlovskii, G.M.4
  • 475
    • 34548548871 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional deaminase/reductase RibD of the riboflavin biosynthetic pathway in Escherichia coli: Implications for the reductive mechanism
    • Stenmark, P., M. Moche, D. Gurmu, and P. Nordlund. 2007. The crystal structure of the bifunctional deaminase/reductase RibD of the riboflavin biosynthetic pathway in Escherichia coli: implications for the reductive mechanism. J. Mol. Biol. 373:48-64.
    • (2007) J. Mol. Biol. , vol.373 , pp. 48-64
    • Stenmark, P.1    Moche, M.2    Gurmu, D.3    Nordlund, P.4
  • 476
    • 0015448259 scopus 로고
    • Mutants of Eremothecium ashbyii resistant to 8-azaguanine. Communication I. Isolation of mutants and study of the level of riboflavin biosynthesis
    • Stepanov, A. I., M. Y. Beburov, and V. G. Zhdanov. 1974. Mutants of Eremothecium ashbyii resistant to 8-azaguanine. Communication I. Isolation of mutants and study of the level of riboflavin biosynthesis. Sov. Genet. 8:729-733.
    • (1974) Sov. Genet. , vol.8 , pp. 729-733
    • Stepanov, A.I.1    Beburov, M.Y.2    Zhdanov, V.G.3
  • 477
    • 0016084733 scopus 로고
    • The use of mutagenic factors in the selection of the riboflavin producer Eremothecium ashbyii
    • Stepanov, A. I., and V. G. Zhdanov. 1974. The use of mutagenic factors in the selection of the riboflavin producer Eremothecium ashbyii. Sov. Genet. 8:745-749.
    • (1974) Sov. Genet. , vol.8 , pp. 745-749
    • Stepanov, A.I.1    Zhdanov, V.G.2
  • 479
    • 0018828677 scopus 로고
    • Riboflavin accumulation by cells of the yeast Pichia (Candida) guilliermondii
    • Straube, G. 1980. Riboflavin accumulation by cells of the yeast Pichia (Candida) guilliermondii. Z. Allg. Mikrobiol. 20:215-218.
    • (1980) Z. Allg. Mikrobiol. , vol.20 , pp. 215-218
    • Straube, G.1
  • 480
    • 0013826475 scopus 로고
    • Intestinal absorption of riboflavin in man
    • Stripp, B. 1975. Intestinal absorption of riboflavin in man. Acta Pharmacol. Toxicol. 22:353-362.
    • (1975) Acta Pharmacol. Toxicol. , vol.22 , pp. 353-362
    • Stripp, B.1
  • 481
    • 0015626893 scopus 로고
    • Purification and some properties of the alkaline phosphatase I of Pichia guilliermondii yeasts
    • In Ukrainian
    • Strugovshchikova, L. P., G. M. Shavlovskii., I. P. Fedorovich, and R. V. Kucheras. 1973. Purification and some properties of the alkaline phosphatase I of Pichia guilliermondii yeasts. Ukr. Biokhim. Zhurn. 45:312-317. (In Ukrainian.)
    • (1973) Ukr. Biokhim. Zhurn. , vol.45 , pp. 312-317
    • Strugovshchikova, L.P.1    Shavlovskii, G.M.2    Fedorovich, I.P.3    Kucheras, R.V.4
  • 482
    • 67349285773 scopus 로고    scopus 로고
    • Importance of malate synthase in the glyoxylate cycle of Ashbya gossypii for the efficient production of riboflavin
    • Sugimoto, T., S. Kanamasa, T. Kato, and E. Y. Park. 2009. Importance of malate synthase in the glyoxylate cycle of Ashbya gossypii for the efficient production of riboflavin. Appl. Microbiol. Biotechnol. 83:529-539.
    • (2009) Appl. Microbiol. Biotechnol. , vol.83 , pp. 529-539
    • Sugimoto, T.1    Kanamasa, S.2    Kato, T.3    Park, E.Y.4
  • 483
    • 76949101812 scopus 로고    scopus 로고
    • Isolation of an oxalate-resistant Ashbya gossypii strain and its improved riboflavin production
    • Sugimoto, T., A. Morimoto, M. Nariyama, T. Kato, and E. Y. Park. 2010. Isolation of an oxalate-resistant Ashbya gossypii strain and its improved riboflavin production. J. Ind. Microbiol. Biotechnol. 37:57-64.
    • (2010) J. Ind. Microbiol. Biotechnol. , vol.37 , pp. 57-64
    • Sugimoto, T.1    Morimoto, A.2    Nariyama, M.3    Kato, T.4    Park, E.Y.5
  • 484
    • 34249907264 scopus 로고    scopus 로고
    • Riboflavin may interfere with on-line monitoring of secreted green fluorescence protein fusion proteins in Pichia pastoris
    • Surribas, A., D. Resina, P. Ferrer, and F. Valero. 2007. Riboflavin may interfere with on-line monitoring of secreted green fluorescence protein fusion proteins in Pichia pastoris. Microb. Cell Fact. 6:15.
    • (2007) Microb. Cell Fact. , vol.6 , pp. 15
    • Surribas, A.1    Resina, D.2    Ferrer, P.3    Valero, F.4
  • 487
    • 78651159260 scopus 로고
    • Studies on dextransucrase. II. Factors affecting the formation of riboflavinylglucoside in growing cultures of Leuconostoc mesenteroides
    • Kyoto
    • Suzuki, Y., and H. Katagiri. 1963. Studies on dextransucrase. II. Factors affecting the formation of riboflavinylglucoside in growing cultures of Leuconostoc mesenteroides. J. Vitaminol. (Kyoto) 10:293-298.
    • (1963) J. Vitaminol. , vol.10 , pp. 293-298
    • Suzuki, Y.1    Katagiri, H.2
  • 489
    • 0036769661 scopus 로고    scopus 로고
    • Influence of manganese on iron accumulation and flavinogenesis in yeast Debaryomyces hansenii
    • In Ukrainian
    • Sydorovych, I. B., and D. V. Fedorovych. 2002. Influence of manganese on iron accumulation and flavinogenesis in yeast Debaryomyces hansenii. Mikrobiol. Z. 64:47-52. (In Ukrainian.)
    • (2002) Mikrobiol. Z. , vol.64 , pp. 47-52
    • Sydorovych, I.B.1    Fedorovych, D.V.2
  • 490
    • 0016727763 scopus 로고
    • Identification of the chemical structures of schizoflavins as 7,8-dimethyl-10-(2,3,4-trihydroxy-4-formylbutyl)isoalloxazine and 7,8-dimethyl-10-(2,3,4-trihydroxy-4-carboxybutyl) isoalloxazine
    • Tachibana, S., T. Murakami, and T. Ninomiya. 1975. Identification of the chemical structures of schizoflavins as 7,8-dimethyl-10-(2,3,4-trihydroxy-4- formylbutyl)isoalloxazine and 7,8-dimethyl-10-(2,3,4-trihydroxy-4-carboxybutyl) isoalloxazine. J. Nutr. Sci. Vitaminol. 21:347-353.
    • (1975) J. Nutr. Sci. Vitaminol. , vol.21 , pp. 347-353
    • Tachibana, S.1    Murakami, T.2    Ninomiya, T.3
  • 492
    • 72049097675 scopus 로고    scopus 로고
    • Riboflavin induces resistance in rice against Rhizoctonia solani via jasmonate-mediated priming of phenylpropanoid pathway
    • Taheri, P., and S. Tarighi. 2010. Riboflavin induces resistance in rice against Rhizoctonia solani via jasmonate-mediated priming of phenylpropanoid pathway. J. Plant Physiol. 167:201-208.
    • (2010) J. Plant Physiol. , vol.167 , pp. 201-208
    • Taheri, P.1    Tarighi, S.2
  • 493
    • 69049101067 scopus 로고    scopus 로고
    • Increased riboflavin production from activated bleaching earth by a mutant strain of Ashbya gossypii
    • Tajima, S., Y. Itoh, T. Sugimoto, T. Kato, and E. Y. Park. 2009. Increased riboflavin production from activated bleaching earth by a mutant strain of Ashbya gossypii. J. Biosci. Biotechnol. 108:325-329.
    • (2009) J. Biosci. Biotechnol. , vol.108 , pp. 325-329
    • Tajima, S.1    Itoh, Y.2    Sugimoto, T.3    Kato, T.4    Park, E.Y.5
  • 494
    • 68049099263 scopus 로고    scopus 로고
    • Discovery and development of a small molecule library with lumazine synthase inhibitory activity
    • Talukdar, A., et al. 2009. Discovery and development of a small molecule library with lumazine synthase inhibitory activity. J. Org. Chem. 74:5123-5134.
    • (2009) J. Org. Chem. , vol.74 , pp. 5123-5134
    • Talukdar, A.1
  • 495
    • 0008148048 scopus 로고
    • Riboflavin production by Candida species
    • Tanner, F. W., Jr., C. Voinovich, and J. M. Van Lanen. 1945. Riboflavin production by Candida species. Science 101:180-181.
    • (1945) Science , vol.101 , pp. 180-181
    • Tanner Jr., F.W.1    Voinovich, C.2    Van Lanen, J.M.3
  • 496
    • 50249172768 scopus 로고    scopus 로고
    • Screening of Bacillus subtilis transposon mutants with altered riboflavin production
    • Tännler, S., N. Zamboni, C. Kiraly, S. Aymerich, and U. Sauer. 2008. Screening of Bacillus subtilis transposon mutants with altered riboflavin production. Metab. Eng. 10:216-226.
    • (2008) Metab. Eng. , vol.10 , pp. 216-226
    • Tännler, S.1    Zamboni, N.2    Kiraly, C.3    Aymerich, S.4    Sauer, U.5
  • 497
    • 67649122123 scopus 로고    scopus 로고
    • Determination of the essential nutrient requirements of wine-related bacteria from the genera Oenococcus and Lactobacillus
    • Terrade, N., and R. Mira de Orduña. 2009. Determination of the essential nutrient requirements of wine-related bacteria from the genera Oenococcus and Lactobacillus. Int. J. Food Microbiol. 133:8-13.
    • (2009) Int. J. Food Microbiol. , vol.133 , pp. 8-13
    • Terrade, N.1    Mira De Orduña, R.2
  • 498
    • 0020820798 scopus 로고
    • Localization of the genes coding for GTP cyclohydrolase II and riboflavin synthase on the chromosome of Escherichia coli K-12
    • In Russian
    • Tesliar, G. E., and G. M. Shavlovskii. 1983. Localization of the genes coding for GTP cyclohydrolase II and riboflavin synthase on the chromosome of Escherichia coli K-12. Tsitol. Genet. 17:54-56. (In Russian.)
    • (1983) Tsitol. Genet. , vol.17 , pp. 54-56
    • Tesliar, G.E.1    Shavlovskii, G.M.2
  • 499
    • 66749094194 scopus 로고    scopus 로고
    • Flavin mononucleotide-based fluorescent protein as an oxygen-independent reporter in Candida albicans and Saccharomyces cerevisiae
    • Tielker, D., I. Eichhof, K. E. Jaeger, and J. F. Ernst. 2009. Flavin mononucleotide-based fluorescent protein as an oxygen-independent reporter in Candida albicans and Saccharomyces cerevisiae. Eukaryot. Cell 8:913-915.
    • (2009) Eukaryot. Cell , vol.8 , pp. 913-915
    • Tielker, D.1    Eichhof, I.2    Jaeger, K.E.3    Ernst, J.F.4
  • 501
    • 79958065176 scopus 로고
    • Biochemical investigation of the properties of a mutant of the methylotrophic yeast Hansenula polymorpha with reduced FAD and alcohol oxidase content
    • Moscow
    • Ubiivovk, V. M., and A. A. Sibirnyi. 1991. Biochemical investigation of the properties of a mutant of the methylotrophic yeast Hansenula polymorpha with reduced FAD and alcohol oxidase content. Biochemistry (Moscow) 56:1570-1576.
    • (1991) Biochemistry , vol.56 , pp. 1570-1576
    • Ubiivovk, V.M.1    Sibirnyi, A.A.2
  • 502
    • 0025354449 scopus 로고
    • Lampteroflavin, the first riboflavinyl alpha ribofuranoside as light emitter in the luminous mushroom, L. japonicus
    • DOI 10.1016/S0040-4020(01)86700-4
    • Uyakul, D., M. Isobe, and T. Goto. 1990. Lampteroflavin, the first riboflavinyl alpha ribofuranoside as light emitter in the luminous mushroom Lampteromyces japonicus. Tetrahedron 46:1367-1378. (Pubitemid 20190940)
    • (1990) Tetrahedron , vol.46 , Issue.4 , pp. 1367-1378
    • Uyakul, D.1    Isobe, M.2    Goto, T.3
  • 503
    • 0025726684 scopus 로고
    • Biosynthesis and assembly of alcohol oxidase, a peroxisomal matrix protein in methylotrophic yeasts: A review
    • van der Klei, I. J., W. Harder, and M. Veenhuis. 1991. Biosynthesis and assembly of alcohol oxidase, a peroxisomal matrix protein in methylotrophic yeasts: a review. Yeast 7:195-209.
    • (1991) Yeast , vol.7 , pp. 195-209
    • Van Der Klei, I.J.1    Harder, W.2    Veenhuis, M.3
  • 505
    • 10344222659 scopus 로고    scopus 로고
    • Riboflavin excretion from the excised roots of Hyoscyamus niger
    • Vardja, T., R. Vardja, K. Pudersell, and A. Tohver. 2004. Riboflavin excretion from the excised roots of Hyoscyamus niger. Pharm. Biol. 42:353-359.
    • (2004) Pharm. Biol. , vol.42 , pp. 353-359
    • Vardja, T.1    Vardja, R.2    Pudersell, K.3    Tohver, A.4
  • 506
    • 12144290342 scopus 로고    scopus 로고
    • Liquid chromatographic analysis of riboflavin vitamers in foods using fluorescence detection
    • Vinas, P., N. Balsalobre, C. Lopez-Erroz, and M. Hernandez-Cordoba. 2004. Liquid chromatographic analysis of riboflavin vitamers in foods using fluorescence detection. J. Agric. Food Chem. 52:1789-1794.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1789-1794
    • Vinas, P.1    Balsalobre, N.2    Lopez-Erroz, C.3    Hernandez-Cordoba, M.4
  • 507
    • 0037100667 scopus 로고    scopus 로고
    • Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation
    • Vitreschak, A. G., D. A. Rodionov, A. A. Mironov, and M. S. Gelfand. 2002. Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation. Nucleic Acids Res. 30:3141-3151.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3141-3151
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 508
    • 35048832520 scopus 로고    scopus 로고
    • 2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum
    • 2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum. J. Bacteriol. 189:7367-7375.
    • (2007) J. Bacteriol. , vol.189 , pp. 7367-7375
    • Vogl, C.1
  • 509
    • 0000439998 scopus 로고
    • Biosynthesis of riboflavin. The structure of the four-carbon precursor
    • Volk, R., and A. Bacher. 1988. Biosynthesis of riboflavin. The structure of the four-carbon precursor. J. Am. Chem. Soc. 110:3651-3653.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3651-3653
    • Volk, R.1    Bacher, A.2
  • 510
    • 0025203677 scopus 로고
    • Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2-butanone-4-phosphate synthase
    • Volk, R., and A. Bacher. 1990. Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2- butanone-4-phosphate synthase. J. Biol. Chem. 265:19479-19485.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19479-19485
    • Volk, R.1    Bacher, A.2
  • 511
    • 0025720052 scopus 로고
    • Biosynthesis of riboflavin. Studies on the mechanism of L-3,4-dihydroxy-2-butanone 4-phosphate synthase
    • Volk, R., and A. Bacher. 1991. Biosynthesis of riboflavin. Studies on the mechanism of L-3,4-dihydroxy-2-butanone 4-phosphate synthase. J. Biol. Chem. 266:20610-20618.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20610-20618
    • Volk, R.1    Bacher, A.2
  • 512
    • 38949214833 scopus 로고    scopus 로고
    • Secretion of flavins by Shewanella species and their role in extracellular electron transfer
    • von Canstein, H., J. Ogawa, S. Shimizu, and J. R. Lloyd. 2008. Secretion of flavins by Shewanella species and their role in extracellular electron transfer. Appl. Environ. Microbiol. 74:615-623.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 615-623
    • Von Canstein, H.1    Ogawa, J.2    Shimizu, S.3    Lloyd, J.R.4
  • 514
    • 0036053160 scopus 로고    scopus 로고
    • Development of a transformation system for the flavinogenic yeast Candida famata
    • Voronovsky, A. Y., et al. 2002. Development of a transformation system for the flavinogenic yeast Candida famata. FEMS Yeast Res. 2:381-388.
    • (2002) FEMS Yeast Res. , vol.2 , pp. 381-388
    • Voronovsky, A.Y.1
  • 516
    • 0001038064 scopus 로고
    • 4-(1′-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second product of the riboflavin synthetase reaction
    • Wacker, H., R. A. Harvey, C. H. Winestock, and G. W. Plaut. 1964. 4-(1′-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second product of the riboflavin synthetase reaction. J. Biol. Chem. 239:3493-3497.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3493-3497
    • Wacker, H.1    Harvey, R.A.2    Winestock, C.H.3    Plaut, G.W.4
  • 517
    • 0000537597 scopus 로고
    • Naturally occurring 5-deazaflavin coenzymes: Biological redox roles
    • Walsh, C. 1986. Naturally occurring 5-deazaflavin coenzymes: biological redox roles. Acc. Chem. Res. 19:216-221.
    • (1986) Acc. Chem. Res. , vol.19 , pp. 216-221
    • Walsh, C.1
  • 518
    • 0017822342 scopus 로고
    • Chemical and enzymatic properties of riboflavin analogues
    • Walsh, C., et al. 1978. Chemical and enzymatic properties of riboflavin analogues. Biochemistry 17:1942-1951. (Pubitemid 8349840)
    • (1978) Biochemistry , vol.17 , Issue.10 , pp. 1942-1951
    • Walsh, C.1    Fisher, J.2    Spencer, R.3
  • 519
    • 41649110406 scopus 로고    scopus 로고
    • Isolation and characterization of Candida membranifaciens subsp. Flavinogenie W14-3, a novel riboflavin-producing marine yeast
    • Wang, L., et al. 2008. Isolation and characterization of Candida membranifaciens subsp. flavinogenie W14-3, a novel riboflavin-producing marine yeast. Microbiol. Res. 163:255-266.
    • (2008) Microbiol. Res. , vol.163 , pp. 255-266
    • Wang, L.1
  • 520
    • 0041919534 scopus 로고    scopus 로고
    • Crystal structure of a flavin-binding protein from Thermotoga maritima
    • Wang, W., R. Kim, J. Jancarik, H. Yokota, and S. H. Kim. 2003. Crystal structure of a flavin-binding protein from Thermotoga maritima. Proteins 52:633-635.
    • (2003) Proteins , vol.52 , pp. 633-635
    • Wang, W.1    Kim, R.2    Jancarik, J.3    Yokota, H.4    Kim, S.H.5
  • 521
    • 10844293516 scopus 로고    scopus 로고
    • Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima
    • Wang, W., R. Kim, H. Yokota, and S. H. Kim. 2005. Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima. Proteins 58:246-248.
    • (2005) Proteins , vol.58 , pp. 246-248
    • Wang, W.1    Kim, R.2    Yokota, H.3    Kim, S.H.4
  • 523
    • 0016380164 scopus 로고
    • Production of flavine-adenine dinucleotide from riboflavine by a mutant of Sarcina lutea
    • Watanabe, T., T. Uchida, J. Kato, and I. Chibata. 1974. Production of flavine-adenine dinucleotide from riboflavine by a mutant of Sarcina lutea. Arch. Microbiol. 27:531-536.
    • (1974) Arch. Microbiol. , vol.27 , pp. 531-536
    • Watanabe, T.1    Uchida, T.2    Kato, J.3    Chibata, I.4
  • 524
    • 33947449544 scopus 로고
    • Chelates, absorption and translocation of ethylenediaminetetraacetic acid by sunflower plants
    • Weinstein, L. H., E. R. Purvis, A. N. Meiss, and R. L. Uhler. 1954. Chelates, absorption and translocation of ethylenediaminetetraacetic acid by sunflower plants. J. Agric. Food Chem. 2:421-424.
    • (1954) J. Agric. Food Chem. , vol.2 , pp. 421-424
    • Weinstein, L.H.1    Purvis, E.R.2    Meiss, A.N.3    Uhler, R.L.4
  • 525
    • 17844362176 scopus 로고    scopus 로고
    • Ashbya gossypii: A model for fungal developmental biology
    • Wendland, J., and A. Walther. 2005. Ashbya gossypii: a model for fungal developmental biology. Nat. Rev. Microbiol. 3:421-429.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 421-429
    • Wendland, J.1    Walther, A.2
  • 527
    • 0035219754 scopus 로고    scopus 로고
    • Biosynthesis of methanogenic cofactors
    • White, R. H. 2001. Biosynthesis of methanogenic cofactors. Vitamins Hormones 61:299-339.
    • (2001) Vitamins Hormones , vol.61 , pp. 299-339
    • White, R.H.1
  • 530
    • 0006174166 scopus 로고
    • Regulation of flavin synthesis by Escherichia coli
    • Wilson, A. C., and A. B. Pardee. 1962. Regulation of flavin synthesis by Escherichia coli. J. Gen. Microbiol. 28:283-303.
    • (1962) J. Gen. Microbiol. , vol.28 , pp. 283-303
    • Wilson, A.C.1    Pardee, A.B.2
  • 531
    • 33746325823 scopus 로고    scopus 로고
    • Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor
    • Winkler, A., F. Hartner, T. M. Kutchan, A. Glieder, and P. Macheroux. 2006. Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor. J. Biol. Chem. 281:21276-21285.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21276-21285
    • Winkler, A.1    Hartner, F.2    Kutchan, T.M.3    Glieder, A.4    Macheroux, P.5
  • 533
    • 0031916447 scopus 로고    scopus 로고
    • Helicobacter pylori ribBA-mediated riboflavin production is involved in iron acquisition
    • Worst, D. J., M. M. Gerrits, C. M. Vandenbrouke-Grauls, and J. G. Kusters. 1998. Helicobacter pylori ribBA-mediated riboflavin production is involved in iron acquisition. J. Bacteriol. 180:1473-1479.
    • (1998) J. Bacteriol. , vol.180 , pp. 1473-1479
    • Worst, D.J.1    Gerrits, M.M.2    Vandenbrouke-Grauls, C.M.3    Kusters, J.G.4
  • 534
    • 0025720559 scopus 로고
    • Replicative transformation of the filamentous fungus Ashbya gossypii with plasmids containing Saccharomyces cerevisiae ARS elements
    • Wright, M. C., and P. Philippsen. 1991. Replicative transformation of the filamentous fungus Ashbya gossypii with plasmids containing Saccharomyces cerevisiae ARS elements. Gene 109:99-105.
    • (1991) Gene , vol.109 , pp. 99-105
    • Wright, M.C.1    Philippsen, P.2
  • 535
    • 0028950476 scopus 로고
    • Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae
    • Wu, M., B. Repetto, D. M. Glerum, and A. Tzagoloff. 1995. Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae. Mol. Cell. Biol. 15:264-271.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 264-271
    • Wu, M.1    Repetto, B.2    Glerum, D.M.3    Tzagoloff, A.4
  • 536
    • 34548319457 scopus 로고    scopus 로고
    • Optimization of riboflavin production by recombinant Bacillus subtilis RH44 using statistical designs
    • Wu, Q. L., T. Chen, Y. Gan, X. Chen, and X. M. Zhao. 2007. Optimization of riboflavin production by recombinant Bacillus subtilis RH44 using statistical designs. Appl. Microbiol. Biotechnol. 76:783-794.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 783-794
    • Wu, Q.L.1    Chen, T.2    Gan, Y.3    Chen, X.4    Zhao, X.M.5
  • 537
    • 77957251410 scopus 로고
    • Separating determination of riboflavin nucleotides by paper electrophoresis
    • Yagi, K., and Y. Matsuoka. 1955. Separating determination of riboflavin nucleotides by paper electrophoresis. J. Biochem. 42:757-762.
    • (1955) J. Biochem. , vol.42 , pp. 757-762
    • Yagi, K.1    Matsuoka, Y.2
  • 538
    • 17944372397 scopus 로고
    • Preparation of flavin adenine dinucleotide from Eremothecium ashbyii
    • Yagi, K., Y. Matsuoka, S. Kuyama, and M. Tada. 1956. Preparation of flavin adenine dinucleotide from Eremothecium ashbyii. J. Biochem. 43:93-100.
    • (1956) J. Biochem. , vol.43 , pp. 93-100
    • Yagi, K.1    Matsuoka, Y.2    Kuyama, S.3    Tada, M.4
  • 540
    • 36949062893 scopus 로고
    • Separation of flavins by ionexchange resins
    • Yagi, K., J. Okuda, and Y. Matsuoka. 1955. Separation of flavins by ionexchange resins. Nature 175:555-556.
    • (1955) Nature , vol.175 , pp. 555-556
    • Yagi, K.1    Okuda, J.2    Matsuoka, Y.3
  • 541
    • 0025304291 scopus 로고
    • Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver
    • Yamada, Y., A. H. Merrill, Jr., and D. B. McCormick. 1990. Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver. Arch. Biochem. Biophys. 278:125-130.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 125-130
    • Yamada, Y.1    Merrill Jr., A.H.2    McCormick, D.B.3
  • 542
    • 67649662425 scopus 로고    scopus 로고
    • Identification and functional characterization of rat riboflavin transporter 2
    • Yamamoto, S., et al. 2009. Identification and functional characterization of rat riboflavin transporter 2. J. Biochem. 145:437-443.
    • (2009) J. Biochem. , vol.145 , pp. 437-443
    • Yamamoto, S.1
  • 543
    • 79958053830 scopus 로고
    • Über die Flavingarung der Aceton-Butylalkoholbakterien
    • Yamasaki, I., and W. Yositome. 1938. Über die Flavingarung der Aceton-Butylalkoholbakterien. Biochem. Z. 297:398.
    • (1938) Biochem. Z. , vol.297 , pp. 398
    • Yamasaki, I.1    Yositome, W.2
  • 545
    • 75749126087 scopus 로고    scopus 로고
    • Medium optimization for production of flavin mononucleotide by the recombinant strain of the yeast Candida famata using statistical designs
    • Yatsyshyn, V. Y., D. V. Fedorovych, and A. A. Sibirny. 2010. Medium optimization for production of flavin mononucleotide by the recombinant strain of the yeast Candida famata using statistical designs. Biochem. Eng. J. 49:52-60.
    • (2010) Biochem. Eng. J. , vol.49 , pp. 52-60
    • Yatsyshyn, V.Y.1    Fedorovych, D.V.2    Sibirny, A.A.3
  • 546
  • 547
    • 69349088255 scopus 로고    scopus 로고
    • Riboflavin kinase couples TNF receptor 1 to NADPH oxidase
    • Yazdanpanah, B., et al. 2009. Riboflavin kinase couples TNF receptor 1 to NADPH oxidase. Nature 460:1159-1163.
    • (2009) Nature , vol.460 , pp. 1159-1163
    • Yazdanpanah, B.1
  • 548
    • 53449091477 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel human and rat riboflavin transporter, RFT1
    • Yonezawa, A., S. Masuda, T. Katsura, and K. Inui. 2008. Identification and functional characterization of a novel human and rat riboflavin transporter, RFT1. Am. J. Physiol. Cell Physiol. 295:C632-C641.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Yonezawa, A.1    Masuda, S.2    Katsura, T.3    Inui, K.4
  • 549
  • 550
    • 0025241849 scopus 로고
    • Cloning of the RIB1 gene coding for the enzyme of the first stage of flavinogenesis in the yeast Pichia guilliermondi, GTP cyclohydrolase, in Escherichia coli cells
    • In Russian
    • Zakalskii, A. E., et al. 1990. Cloning of the RIB1 gene coding for the enzyme of the first stage of flavinogenesis in the yeast Pichia guilliermondi, GTP cyclohydrolase, in Escherichia coli cells. Genetika 26:614-620. (In Russian.)
    • (1990) Genetika , vol.26 , pp. 614-620
    • Zakalskii, A.E.1
  • 551
    • 6044240910 scopus 로고    scopus 로고
    • The phosphoenolpyruvate carboxykinase also catalyzes C3 carboxylation at the interface of glycolysis and the TCA cycle of Bacillus subtilis
    • Zamboni, N., H. Maaheimo, T. Szyperski, H. P. Hohmann, and U. Sauer. 2004. The phosphoenolpyruvate carboxykinase also catalyzes C3 carboxylation at the interface of glycolysis and the TCA cycle of Bacillus subtilis. Metab. Eng. 6:277-284.
    • (2004) Metab. Eng. , vol.6 , pp. 277-284
    • Zamboni, N.1    Maaheimo, H.2    Szyperski, T.3    Hohmann, H.P.4    Sauer, U.5
  • 552
    • 0038514064 scopus 로고    scopus 로고
    • Reducing maintenance metabolism by metabolic engineering of respiration improves riboflavin production by Bacillus subtilis
    • Zamboni, N., N. Mouncey, H. P. Hohmann, and U. Sauer. 2003. Reducing maintenance metabolism by metabolic engineering of respiration improves riboflavin production by Bacillus subtilis. Metab. Eng. 5:49-55.
    • (2003) Metab. Eng. , vol.5 , pp. 49-55
    • Zamboni, N.1    Mouncey, N.2    Hohmann, H.P.3    Sauer, U.4
  • 553
    • 34547789907 scopus 로고    scopus 로고
    • Biochemical fluorometric method for the determination of riboflavin in milk
    • Zandomeneghi, M., L. Carbonaro, and G. Zandomeneghi. 2007. Biochemical fluorometric method for the determination of riboflavin in milk. J. Agric. Food Chem. 55:5990-5994.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5990-5994
    • Zandomeneghi, M.1    Carbonaro, L.2    Zandomeneghi, G.3
  • 554
    • 58949096797 scopus 로고    scopus 로고
    • Riboflavin-induced priming for pathogen defense in Arabidopsis thaliana
    • Zhang, S., et al. 2009. Riboflavin-induced priming for pathogen defense in Arabidopsis thaliana. J. Integr. Plant Biol. 51:167-174.
    • (2009) J. Integr. Plant Biol. , vol.51 , pp. 167-174
    • Zhang, S.1
  • 555
    • 0037453317 scopus 로고    scopus 로고
    • A structure-based model of the reaction catalyzed by lumazine synthase from Aquifex aeolicus
    • Zhang, X., et al. 2003. A structure-based model of the reaction catalyzed by lumazine synthase from Aquifex aeolicus. J. Mol. Biol. 328:167-182.
    • (2003) J. Mol. Biol. , vol.328 , pp. 167-182
    • Zhang, X.1
  • 556
    • 0035830969 scopus 로고    scopus 로고
    • X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: Determinants of thermostability revealed from structural comparisons
    • Zhang, X., W. Meining, M. Fischer, A. Bacher, and R. Ladenstein. 2001. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons. J. Mol. Biol. 306:1099-1114.
    • (2001) J. Mol. Biol. , vol.306 , pp. 1099-1114
    • Zhang, X.1    Meining, W.2    Fischer, M.3    Bacher, A.4    Ladenstein, R.5
  • 557
    • 68049092045 scopus 로고    scopus 로고
    • Discovery and development of the covalent hydrates of trifluoromethylated pyrazoles as riboflavin synthase inhibitors with antibiotic activity against Mycobacterium tuberculosis
    • Zhao, Y., et al. 2009. Discovery and development of the covalent hydrates of trifluoromethylated pyrazoles as riboflavin synthase inhibitors with antibiotic activity against Mycobacterium tuberculosis. J. Org. Chem. 74:5297-5303.
    • (2009) J. Org. Chem. , vol.74 , pp. 5297-5303
    • Zhao, Y.1
  • 558
    • 33845649466 scopus 로고    scopus 로고
    • Enhancement of riboflavin production by overexpression of acetolactate synthase in a pta mutant of Bacillus subtilis
    • Zhu, Y., X. Chen, T. Chen, and X. Zhao. 2007. Enhancement of riboflavin production by overexpression of acetolactate synthase in a pta mutant of Bacillus subtilis. FEMS Microbiol. Lett. 266:224-230.
    • (2007) FEMS Microbiol. Lett. , vol.266 , pp. 224-230
    • Zhu, Y.1    Chen, X.2    Chen, T.3    Zhao, X.4
  • 559
    • 64349092621 scopus 로고    scopus 로고
    • Transport of high concentration of thiamin, riboflavin and pyridoxine across intestinal epithelial cells Caco-2
    • Tokyo
    • Zielińska-Dawidziak, M., K. Grajek, A. Olejnik, K. Czaczyk, and W. Grajek. 2008. Transport of high concentration of thiamin, riboflavin and pyridoxine across intestinal epithelial cells Caco-2. J. Nutr. Sci. Vitaminol. (Tokyo) 54:423-429.
    • (2008) J. Nutr. Sci. Vitaminol. , vol.54 , pp. 423-429
    • Zielińska-Dawidziak, M.1    Grajek, K.2    Olejnik, A.3    Czaczyk, K.4    Grajek, W.5
  • 560
    • 33748994291 scopus 로고    scopus 로고
    • 2 biosynthesis: 6,7-dimethyl-8- ribityllumazine synthases of Brucella
    • 2 biosynthesis: 6,7-dimethyl-8-ribityllumazine synthases of Brucella. J. Bacteriol. 188:6135-6142.
    • (2006) J. Bacteriol. , vol.188 , pp. 6135-6142
    • Zylberman, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.