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Volumn 466, Issue , 2015, Pages 137-145

A directed-overflow and damage-control N-glycosidase in riboflavin biosynthesis

Author keywords

Arabidopsis thaliana; Maillard cascade; Metabolite damage; Vibrio vulnificus; Vitamin B2; Zea mays

Indexed keywords

BACTERIAL PROTEIN; COG3236 PROTEIN; GLYCOSIDASE; RIBA PROTEIN; RIBOFLAVIN; RIBOFLAVIN BINDING PROTEIN; UNCLASSIFIED DRUG; ISOENZYME; VEGETABLE PROTEIN;

EID: 84922327064     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141237     Document Type: Article
Times cited : (39)

References (56)
  • 1
    • 84881475919 scopus 로고    scopus 로고
    • Pyrimidine homeostasis is accomplished by directed overflow metabolism
    • Reaves, M. L., Young, B. D., Hosios, A. M., Xu, Y. F. and Rabinowitz, J. D. (2013) Pyrimidine homeostasis is accomplished by directed overflow metabolism. Nature 500, 237-241
    • (2013) Nature , vol.500 , pp. 237-241
    • Reaves, M.L.1    Young, B.D.2    Hosios, A.M.3    Xu, Y.F.4    Rabinowitz, J.D.5
  • 3
    • 77954237941 scopus 로고    scopus 로고
    • Homocysteine methyltransferases Mht1 and Sam4 prevent the accumulation of age-damaged (R,S) -AdoMet in the yeast Saccharomyces cerevisiae
    • Vinci, C. R. and Clarke, S. G. (2010) Homocysteine methyltransferases Mht1 and Sam4 prevent the accumulation of age-damaged (R,S) -AdoMet in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 285, 20526-20531
    • (2010) J. Biol. Chem. , vol.285 , pp. 20526-20531
    • Vinci, C.R.1    Clarke, S.G.2
  • 4
    • 84891632259 scopus 로고    scopus 로고
    • The logic of metabolism and its fuzzy consequences
    • Danchin, A. and Sekowska, A. (2014) The logic of metabolism and its fuzzy consequences. Environ. Microbiol. 16, 19-28
    • (2014) Environ. Microbiol. , vol.16 , pp. 19-28
    • Danchin, A.1    Sekowska, A.2
  • 5
    • 0000588548 scopus 로고    scopus 로고
    • The other side of metabolism: A review
    • Golubev, A. G. (1996) The other side of metabolism: a review. Biochemistry (Mosc.) 61, 2018-2039
    • (1996) Biochemistry (Mosc.) , vol.61 , pp. 2018-2039
    • Golubev, A.G.1
  • 6
    • 77956925998 scopus 로고    scopus 로고
    • Messy biology and the origins of evolutionary innovations
    • PubMed
    • Tawfik, D. S. (2010) Messy biology and the origins of evolutionary innovations. Nat. Chem. Biol. 6, 692-696 PubMed
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 692-696
    • Tawfik, D.S.1
  • 7
    • 21244445102 scopus 로고    scopus 로고
    • Biosynthesis of flavocoenzymes
    • Fischer, M. and Bacher, A. (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
  • 9
    • 4344648767 scopus 로고    scopus 로고
    • Evolution of vitamin B2 biosynthesis: Structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin
    • Fischer, M., R ömisch, W., Saller, S., Illarionov, B., Richter, G., Rohdich, F., Eisenreich, W. and Bacher, A. (2004) Evolution of vitamin B2 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    Ömisch W, R.2    Saller, S.3    Illarionov, B.4    Richter, G.5    Rohdich, F.6    Eisenreich, W.7    Bacher, A.8
  • 10
    • 0016789502 scopus 로고
    • Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli
    • PubMed
    • Foor, F. and Brown, G. M. (1975) Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. J. Biol. Chem. 250, 3545-3551 PubMed
    • (1975) J. Biol. Chem. , vol.250 , pp. 3545-3551
    • Foor, F.1    Brown, G.M.2
  • 11
    • 45749137952 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of the Escherichia coli ribD -encoded bifunctional deaminase-reductase involved in riboflavin biosynthesis
    • Magalhaäes, M. L., Argyrou, A., Cahill, S. M. and Blanchard, J. S. (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
    • Magalhaäes, M.L.1    Argyrou, A.2    Cahill, S.M.3    Blanchard, J.S.4
  • 12
    • 77957909920 scopus 로고    scopus 로고
    • The photosensitive phs1 mutant is impaired in the riboflavin biogenesis pathway
    • Ouyang, M., Ma, J., Zou, M., Guo, J., Wang, L., Lu, C. and Zhang, L. (2010) The photosensitive phs1 mutant is impaired in the riboflavin biogenesis pathway. J. Plant Physiol. 167, 1466-1476
    • (2010) J. Plant Physiol. , vol.167 , pp. 1466-1476
    • Ouyang, M.1    Ma, J.2    Zou, M.3    Guo, J.4    Wang, L.5    Lu, C.6    Zhang, L.7
  • 14
    • 84861134293 scopus 로고    scopus 로고
    • Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions
    • de Souza, R. F. and Aravind, L. (2012) Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions. Mol. Biosyst. 8, 1661-1677
    • (2012) Mol. Biosyst. , vol.8 , pp. 1661-1677
    • De Souza, R.F.1    Aravind, L.2
  • 15
    • 36549015556 scopus 로고    scopus 로고
    • Inference of gene function based on gene fusion events: The Rosetta-stone method
    • Suhre, K. (2007) Inference of gene function based on gene fusion events: the Rosetta-stone method. Methods Mol. Biol. 396, 31-41
    • (2007) Methods Mol. Biol. , vol.396 , pp. 31-41
    • Suhre, K.1
  • 16
    • 34249683768 scopus 로고    scopus 로고
    • Tight modulation of Escherichia coli bacterial biofilm formation through controlled expression of adhesion factors
    • Da Re, S., Le Qu ér é, B., Ghigo, J. M. and Beloin, C. (2007) Tight modulation of Escherichia coli bacterial biofilm formation through controlled expression of adhesion factors. Appl. Environ. Microbiol. 73, 3391-3403
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3391-3403
    • Da Re, S.1    Le Quéré, B.2    Ghigo, J.M.3    Beloin, C.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0030946770 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: Characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis
    • PubMed
    • Richter, G., Fischer, M., Krieger, C., Eberhardt, S., Lüttgen, H., Gerstenschl ?ager, I. and Bacher, A. (1997) Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis. J. Bacteriol. 179, 2022-2028 PubMed
    • (1997) J. Bacteriol. , vol.179 , pp. 2022-2028
    • Richter, G.1    Fischer, M.2    Krieger, C.3    Eberhardt, S.4    Lüttgen, H.5    Gerstenschläger, I.6    Bacher, A.7
  • 22
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S. J. and Bent, A. F. (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 23
    • 84890191227 scopus 로고    scopus 로고
    • Description of a riboflavin biosynthetic gene variant prevalent in the phylum Proteobacteria
    • Brutinel, E. D., Dean, A. M. and Gralnick, J. A. (2013) Description of a riboflavin biosynthetic gene variant prevalent in the phylum Proteobacteria. J. Bacteriol. 195, 5479-5486
    • (2013) J. Bacteriol. , vol.195 , pp. 5479-5486
    • Brutinel, E.D.1    Dean, A.M.2    Gralnick, J.A.3
  • 26
    • 19744379886 scopus 로고    scopus 로고
    • Purification and characterization of RihC, a xanthosine-inosine-uridine-adenosine-preferring hydrolase from Salmonella enterica serovar Typhimurium
    • Hansen, M. R. and Dandanell, G. (2005) Purification and characterization of RihC, a xanthosine-inosine-uridine-adenosine-preferring hydrolase from Salmonella enterica serovar Typhimurium. Biochim. Biophys. Acta 1723, 55-62
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 55-62
    • Hansen, M.R.1    Dandanell, G.2
  • 27
    • 79958097953 scopus 로고    scopus 로고
    • The moderately efficient enzyme: Evolutionary and physicochemical trends shaping enzyme parameters
    • Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S. and Milo, R. (2011) The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry 50, 4402-4410
    • (2011) Biochemistry , vol.50 , pp. 4402-4410
    • Bar-Even, A.1    Noor, E.2    Savir, Y.3    Liebermeister, W.4    Davidi, D.5    Tawfik, D.S.6    Milo, R.7
  • 32
    • 0029054040 scopus 로고
    • Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis
    • Kis, K. and Bacher, A. (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
  • 33
    • 61849165016 scopus 로고    scopus 로고
    • The proline dependent transcription factor Put3 regulates the expression of the riboflavin transporter MCH5 in Saccharomyces cerevisiae
    • Spitzner, A., Perzlmaier, A. F., Geillinger, K. E., Reihl, P. and Stolz, J. (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
  • 35
    • 84878262804 scopus 로고    scopus 로고
    • The lumazine synthase/riboflavin synthase complex: Shapes and functions of a highly variable enzyme system
    • Ladenstein, R. M., Fischer, M. and Bacher, A. (2013) The lumazine synthase/riboflavin synthase complex: shapes and functions of a highly variable enzyme system. FEBS J. 280, 2537-2563
    • (2013) FEBS J. , vol.280 , pp. 2537-2563
    • Ladenstein, R.M.1    Fischer, M.2    Bacher, A.3
  • 36
    • 0001216314 scopus 로고
    • Mutarotation, hydrolysis, and rearrangement of glycosylamines
    • Isbell, H. S. and Frush, H. J. (1958) Mutarotation, hydrolysis, and rearrangement of glycosylamines. J. Org. Chem. 23, 1309-1319
    • (1958) J. Org. Chem. , vol.23 , pp. 1309-1319
    • Isbell, H.S.1    Frush, H.J.2
  • 37
  • 38
    • 0014962796 scopus 로고
    • Biosynthesis of riboflavin. Formation of 2,5-diamino-6-hydroxy-4-(1'-D-ribitylamino)pyrimidine in a riboflavin auxotroph
    • PubMed
    • Bacher, A. and Lingens, F. (1970) Biosynthesis of riboflavin. Formation of 2,5-diamino-6-hydroxy-4-(1'-D-ribitylamino)pyrimidine in a riboflavin auxotroph. J. Biol. Chem. 245, 4647-4652 PubMed
    • (1970) J. Biol. Chem. , vol.245 , pp. 4647-4652
    • Bacher, A.1    Lingens, F.2
  • 39
    • 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
  • 40
    • 0024278406 scopus 로고
    • Characterization and chemical properties of phosphoribosylamine, an unstable intermediate in the de novo purine biosynthetic pathway
    • Schendel, F. J., Cheng, Y. S., Otvos, J. D., Wehrli, S. and Stubbe, J. (1988) Characterization and chemical properties of phosphoribosylamine, an unstable intermediate in the de novo purine biosynthetic pathway. Biochemistry 27, 2614-2623
    • (1988) Biochemistry , vol.27 , pp. 2614-2623
    • Schendel, F.J.1    Cheng, Y.S.2    Otvos, J.D.3    Wehrli, S.4    Stubbe, J.5
  • 41
    • 0014295278 scopus 로고
    • On the prediction of pK a values of amino sugars
    • Inouye, S. (1968) On the prediction of pK a values of amino sugars. Chem. Pharm. Bull. 16, 1134-1137
    • (1968) Chem. Pharm. Bull. , vol.16 , pp. 1134-1137
    • Inouye, S.1
  • 42
    • 38949135227 scopus 로고    scopus 로고
    • Relation between triketone structure, generation of reactive oxygen species, and selective toxicity of the diabetogenic agent alloxan
    • Elsner, M., Gurgul-Convey, E. and Lenzen, S. (2008) Relation between triketone structure, generation of reactive oxygen species, and selective toxicity of the diabetogenic agent alloxan. Antioxid. Redox Signal. 10, 691-699
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 691-699
    • Elsner, M.1    Gurgul-Convey, E.2    Lenzen, S.3
  • 43
    • 23744501806 scopus 로고    scopus 로고
    • Maillard reactions of ribose 5-phosphate and amino acids
    • Sandwick, R., Johanson, M. and Breuer, E. (2005) Maillard reactions of ribose 5-phosphate and amino acids. Ann. N.Y. Acad. Sci. 1043, 85-96
    • (2005) Ann. N.Y. Acad. Sci. , vol.1043 , pp. 85-96
    • Sandwick, R.1    Johanson, M.2    Breuer, E.3
  • 44
    • 33749016265 scopus 로고    scopus 로고
    • A general method for selection of riboflavin-overproducing food grade micro-organisms
    • Burgess, C. M., Smid, E. J., Rutten, G. and van Sinderen, D. (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
  • 45
    • 0034091478 scopus 로고    scopus 로고
    • Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production
    • Stahmann, K. P., Revuelta, J. L. and Seulberger, H. (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
  • 46
    • 0033040385 scopus 로고    scopus 로고
    • GTP cyclohydrolase II and 3,4-dihydroxy-2- butanone 4-phosphate synthase are the rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production
    • Hümbelin, M., Griesser, V., Keller, T., Schurter, W., Haiker, M., Hohmann, H. P., Ritz, H., Richter, G., Bacher, A. and van Loon, A. P. (1999) GTP cyclohydrolase II and 3,4-dihydroxy-2- butanone 4-phosphate synthase are the 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    Griesser, V.2    Keller, T.3    Schurter, W.4    Haiker, M.5    Hohmann, H.P.6    Ritz, H.7    Richter, G.8    Bacher, A.9    Van Loon, A.P.10
  • 47
    • 84055193071 scopus 로고    scopus 로고
    • Ribose 5-phosphate glycation reduces cytochrome c respiratory activity and membrane affinity
    • Hildick-Smith, G. J., Downey, M. C., Gretebeck, L. M., Gersten, R. A. and Sandwick, R. K. (2011) Ribose 5-phosphate glycation reduces cytochrome c respiratory activity and membrane affinity. Biochemistry 50, 11047-11057
    • (2011) Biochemistry , vol.50 , pp. 11047-11057
    • Hildick-Smith, G.J.1    Downey, M.C.2    Gretebeck, L.M.3    Gersten, R.A.4    Sandwick, R.K.5
  • 48
    • 21744454994 scopus 로고    scopus 로고
    • Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme
    • Fortpied, J., Gemayel, R., Stroobant, V. and van Schaftingen, E. (2005) Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme. Biochem. J. 388, 795-802
    • (2005) Biochem. J. , vol.388 , pp. 795-802
    • Fortpied, J.1    Gemayel, R.2    Stroobant, V.3    Van Schaftingen, E.4
  • 49
    • 0024788499 scopus 로고
    • Gratuitous induction of xanthine oxidase by 5,6-diaminouracil in continuously grown cells of Arthrobacter globiformis M4
    • Middelhoven, W. J., Brons, H. J., Breedveld, M. W., Suy, I. M. and van der Plas, H. C. (1989) Gratuitous induction of xanthine oxidase by 5,6-diaminouracil in continuously grown cells of Arthrobacter globiformis M4. Appl. Microbiol. Biotechnol. 32, 323-326
    • (1989) Appl. Microbiol. Biotechnol. , vol.32 , pp. 323-326
    • Middelhoven, W.J.1    Brons, H.J.2    Breedveld, M.W.3    Suy, I.M.4    Van Der Plas, H.C.5
  • 50
    • 34250523325 scopus 로고
    • Formation of 4,5- iaminouracil in a riboflavineless mutant of Aspergillus nidulans
    • Sadique, J., Shanmugasundaram, R. and Shanmugasundaram, E. R. (1966) Formation of 4,5- iaminouracil in a riboflavineless mutant of Aspergillus nidulans. Naturwissenschaften 53, 282
    • (1966) Naturwissenschaften , vol.53 , pp. 282
    • Sadique, J.1    Shanmugasundaram, R.2    Shanmugasundaram, E.R.3
  • 51
    • 0015240352 scopus 로고
    • Biosynthesis of riboflavin. Formation of 6-hydroxy-2,4,5-triamino-pyrimidine in Rib7 mutants of Saccharomyces cerevisiae
    • PubMed
    • Bacher, A. and Lingens, F. (1971) Biosynthesis of riboflavin. Formation of 6-hydroxy-2,4,5-triamino-pyrimidine in Rib7 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 246, 7018-7022 PubMed
    • (1971) J. Biol. Chem. , vol.246 , pp. 7018-7022
    • Bacher, A.1    Lingens, F.2
  • 52
    • 68149170547 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin. Screening for an improved GTP cyclohydrolase II mutant
    • Lehmann, M., Degen, S., Hohmann, H. P., Wyss, M., Bacher, A. and Schramek, N. (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    Degen, S.2    Hohmann, H.P.3    Wyss, M.4    Bacher, A.5    Schramek, N.6
  • 53
    • 39749110672 scopus 로고    scopus 로고
    • Understanding functional divergence in proteins by studying intragenomic homologues
    • Spoonamore, J. E. and Bandarian, V. (2008) Understanding functional divergence in proteins by studying intragenomic homologues. Biochemistry 47, 2592-2600
    • (2008) Biochemistry , vol.47 , pp. 2592-2600
    • Spoonamore, J.E.1    Bandarian, V.2
  • 54
    • 0018087061 scopus 로고
    • Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
    • PubMed
    • Burrows, R. B. and Brown, G. M. (1978) Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136, 657-667 PubMed
    • (1978) J. Bacteriol. , vol.136 , pp. 657-667
    • Burrows, R.B.1    Brown, G.M.2


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