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Volumn 180, Issue 6, 2003, Pages 455-464

Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F420 biosynthesis

Author keywords

4 Hydroxyphenylpyruvate; 7,8 Didemethyl 8 hydroxy 5 deazariboflavin; Coenzyme F 420; FO synthase; Methanocaldococcus jannaschii; Mycobacterium smegmatis; Radical reaction; Riboflavin; S adenosylmethionine

Indexed keywords

4 HYDROXYPHENYLPYRUVIC ACID; 7,8 DINOR 8 HYDROXY 5 DEAZARIBOFLAVIN; 7,8 DINOR 8 HYDROXY 5 DEAZARIBOFLAVIN SYNTHASE; COENZYME F420; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; ENZYME; FERROUS ION; GENE PRODUCT; PHENYLPYRUVIC ACID; PROTEIN COFG; PROTEIN COFH; PROTEIN SUBUNIT; PYRIMIDINE; RIBOFLAVIN DERIVATIVE; RIBOFLAVIN SYNTHASE; S ADENOSYLMETHIONINE; SULFIDE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0347625651     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-003-0614-8     Document Type: Article
Times cited : (60)

References (49)
  • 2
    • 0019143005 scopus 로고
    • Synthesis of 8-demethyl-8-hydroxy-5-deazariboflavins
    • Ashton WT, Brown RD (1980) Synthesis of 8-demethyl-8-hydroxy-5- deazariboflavins. J Heterocyclic Chem 17:1709-1712
    • (1980) J Heterocyclic Chem , vol.17 , pp. 1709-1712
    • Ashton, W.T.1    Brown, R.D.2
  • 3
    • 0022559123 scopus 로고
    • Heavy riboflavin synthase from Bacillus subtilis
    • Bacher A (1986) Heavy riboflavin synthase from Bacillus subtilis. Methods Enzymol 122:192-199
    • (1986) Methods Enzymol , vol.122 , pp. 192-199
    • Bacher, A.1
  • 5
    • 0014690910 scopus 로고
    • Thyroidal phenylpyruvate tautomerase. Isolation and characterization
    • Blasi F, Fragomele F, Covelli I (1969) Thyroidal phenylpyruvate tautomerase. Isolation and characterization. J Biol Chem 244: 4864-4870
    • (1969) J Biol Chem , vol.244 , pp. 4864-4870
    • Blasi, F.1    Fragomele, F.2    Covelli, I.3
  • 6
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1017-1140
    • (1996) Science , vol.273 , pp. 1017-1140
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5    Sutton, G.G.6
  • 7
    • 0014934316 scopus 로고
    • Model reactions for the biosynthesis of thyroxine. Nonenzymic formation of 3,5,3′-triiodothyronine from 4-hydroxy-3-iodophenylpyruvic acid, 3,5-diiodotyrosine, and oxygen
    • Cahnmann HJ, Funakoshi K (1970) Model reactions for the biosynthesis of thyroxine. Nonenzymic formation of 3,5,3′-triiodothyronine from 4-hydroxy-3-iodophenylpyruvic acid, 3,5-diiodotyrosine, and oxygen. Biochemistry 9:90-98
    • (1970) Biochemistry , vol.9 , pp. 90-98
    • Cahnmann, H.J.1    Funakoshi, K.2
  • 8
    • 0034841061 scopus 로고    scopus 로고
    • Adenosylmethionine-dependent iron-sulfur enzymes: Versatile clusters in a radical new role
    • Cheek J, Broderick JB (2001) Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role. J Biol Inorg Chem 6:209-226
    • (2001) J Biol Inorg Chem , vol.6 , pp. 209-226
    • Cheek, J.1    Broderick, J.B.2
  • 9
    • 0015413829 scopus 로고
    • Isolation and properties of a fluorescent compound, factor 420, from Methanobacterium strain M.o.H
    • Cheeseman P, Toms-Wood A, Wolfe RS (1972) Isolation and properties of a fluorescent compound, factor 420, from Methanobacterium strain M.o.H. J Bacteriol 112:527-531
    • (1972) J Bacteriol , vol.112 , pp. 527-531
    • Cheeseman, P.1    Toms-Wood, A.2    Wolfe, R.S.3
  • 12
    • 0008854776 scopus 로고
    • The prosthetic group of a chromoprotein from Mycobacteria
    • Cousins FB (1960) The prosthetic group of a chromoprotein from Mycobacteria. Biochim Biophys Acta 40:532-534
    • (1960) Biochim Biophys Acta , vol.40 , pp. 532-534
    • Cousins, F.B.1
  • 13
    • 0010371685 scopus 로고
    • 8-Hydroxy-5-deazaflavin-dependent electron transfer in the extreme halophile Halobacterium cutirubrum
    • De Wit LEA, Eker APM (1987) 8-Hydroxy-5-deazaflavin-dependent electron transfer in the extreme halophile Halobacterium cutirubrum. FEMS Microbiol Lett 48:121-125
    • (1987) FEMS Microbiol Lett , vol.48 , pp. 121-125
    • De Wit, L.E.A.1    Eker, A.P.M.2
  • 15
    • 0030956640 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: An unusual riboflavin synthase of Methanobacterium thermoautotrophicum
    • Eberhardt S, Korn S, Lottspeich F, Bacher A (1997) Biosynthesis of riboflavin: an unusual riboflavin synthase of Methanobacterium thermoautotrophicum. J Bacteriol 179:2938-2943
    • (1997) J Bacteriol , vol.179 , pp. 2938-2943
    • Eberhardt, S.1    Korn, S.2    Lottspeich, F.3    Bacher, A.4
  • 17
    • 0025741229 scopus 로고
    • Biosynthesis of nucleotides, flavins, and deazaflavins in Methanobacterium thermoautotrophicum
    • Eisenreich W, Schwarzkopf B, Bacher A (1991) Biosynthesis of nucleotides, flavins, and deazaflavins in Methanobacterium thermoautotrophicum. J Biol Chem 266:9622-9631
    • (1991) J Biol Chem , vol.266 , pp. 9622-9631
    • Eisenreich, W.1    Schwarzkopf, B.2    Bacher, A.3
  • 18
    • 0025272139 scopus 로고
    • DNA photore-activating enzyme from the cyanobacterium Anacystis nidulans
    • Eker AP, Kooiman P, Hessels JK, Yasui A (1990) DNA photore-activating enzyme from the cyanobacterium Anacystis nidulans. J Biol Chem 265:8009-8015
    • (1990) J Biol Chem , vol.265 , pp. 8009-8015
    • Eker, A.P.1    Kooiman, P.2    Hessels, J.K.3    Yasui, A.4
  • 19
    • 0003437299 scopus 로고    scopus 로고
    • 3.6a2.1 edn. Department of Genetics, University of Washington, Seattle
    • Felsenstein J (2001) PHYLIP (phylogeny inference package). In, 3.6a2.1 edn. Department of Genetics, University of Washington, Seattle
    • (2001) PHYLIP (Phylogeny Inference Package)
    • Felsenstein, J.1
  • 20
    • 0002387069 scopus 로고
    • The addition and substitution chemistry of quionines
    • Patai S (ed) Wiley, London
    • Finley KT (1974) The addition and substitution chemistry of quionines. In: Patai S (ed) The chemistry of the quinonoid compounds. Wiley, London, pp 877-1144
    • (1974) The Chemistry of the Quinonoid Compounds , pp. 877-1144
    • Finley, K.T.1
  • 21
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • Frey PA (2001) Radical mechanisms of enzymatic catalysis. Annu Rev Biochem 70:121-148
    • (2001) Annu Rev Biochem , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 22
    • 0033490019 scopus 로고    scopus 로고
    • Electrochemical oxidation of 6-hydroxy-2,4,5-triaminopyrimidine at pyrolytic graphite electrode
    • Goyal RN, Kumar A, Jain N, Gupta P (1999) Electrochemical oxidation of 6-hydroxy-2,4,5-triaminopyrimidine at pyrolytic graphite electrode. Indian J Chem 38A:1015-1023
    • (1999) Indian J Chem , vol.38 A , pp. 1015-1023
    • Goyal, R.N.1    Kumar, A.2    Jain, N.3    Gupta, P.4
  • 23
    • 0036005602 scopus 로고    scopus 로고
    • Elucidation of methanogenic coenzyme biosyntheses: From spectroscopy to genomics
    • Graham DE, White RH (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
  • 24
    • 0037134521 scopus 로고    scopus 로고
    • Identification of coenzyme M biosynthetic phosphosulfolactate synthase. A new family of sulfonate-biosynthesizing enzymes
    • Graham DE, Xu H, White RH (2002) Identification of coenzyme M biosynthetic phosphosulfolactate synthase. A new family of sulfonate- biosynthesizing enzymes. J Biol Chem 277:13421-13429
    • (2002) J Biol Chem , vol.277 , pp. 13421-13429
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 25
    • 0038104341 scopus 로고    scopus 로고
    • 420 analogs contain a terminal a-linked glutamate
    • 420 analogs contain a terminal a-linked glutamate. J Bacteriol 185:4662-4665
    • (2003) J Bacteriol , vol.185 , pp. 4662-4665
    • Graupner, M.1    White, R.H.2
  • 26
    • 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
  • 27
    • 0037336946 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin in archaea, 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii
    • Haase I, Mörtl S, Köhler P, Bacher A, Fischer M (2003) Biosynthesis of riboflavin in archaea, 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur J Biochem 270: 1025-1032
    • (2003) Eur J Biochem , vol.270 , pp. 1025-1032
    • Haase, I.1    Mörtl, S.2    Köhler, P.3    Bacher, A.4    Fischer, M.5
  • 28
    • 0017666039 scopus 로고
    • Flavin and 5-deazaflavin: A chemical evaluation of 'modified' flavoproteins with respect to the mechanisms of redox biocatalysis
    • Hemmerich P, Massey V, Fenner H (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
  • 29
    • 0036507965 scopus 로고    scopus 로고
    • Electrohydrogenation of 4-amino-5-nitrosodimethyluracil with a foamed nickel cathode
    • Hu XE, Yang HW, Wang XJ, Bai RS (2002) Electrohydrogenation of 4-amino-5-nitrosodimethyluracil with a foamed nickel cathode. J Appl Electrochem 32:321-328
    • (2002) J Appl Electrochem , vol.32 , pp. 321-328
    • Hu, X.E.1    Yang, H.W.2    Wang, X.J.3    Bai, R.S.4
  • 30
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X, Holden HM, Raushel FM (2001) Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu Rev Biochem 70:149-180
    • (2001) Annu Rev Biochem , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 32
    • 0035980822 scopus 로고    scopus 로고
    • Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Kaneko T, Nakamura Y, Wolk CP, Kuritz T, Sasamoto S, Watanabe A et al. (2001) Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 8:205-213; 227-253
    • (2001) DNA Res , vol.8 , pp. 205-213
    • Kaneko, T.1    Nakamura, Y.2    Wolk, C.P.3    Kuritz, T.4    Sasamoto, S.5    Watanabe, A.6
  • 34
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form
    • Kulzer R, Pils T, Kappl R, Hüttermann J, Knappe J (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form. J Biol Chem 273:4897-4903
    • (1998) J Biol Chem , vol.273 , pp. 4897-4903
    • Kulzer, R.1    Pils, T.2    Kappl, R.3    Hüttermann, J.4    Knappe, J.5
  • 35
    • 0001173003 scopus 로고    scopus 로고
    • Some common methods in mycobacterial genetics
    • Hatfull GF, Jacobs WRJ (eds) ASM Press, Washington, DC
    • Larsen MH (2000) Some common methods in mycobacterial genetics. In: Hatfull GF, Jacobs WRJ (eds) Molecular genetics of mycobacteria. ASM Press, Washington, DC, p 316
    • (2000) Molecular Genetics of Mycobacteria , pp. 316
    • Larsen, M.H.1
  • 37
    • 0022556269 scopus 로고
    • 420 and its γ-monoglutamyl derivative in nonmethanogenic archaebacteria
    • 420 and its γ-monoglutamyl derivative in nonmethanogenic archaebacteria. J Bacteriol 168:444-448
    • (1986) J Bacteriol , vol.168 , pp. 444-448
    • Lin, X.-L.1    White, R.H.2
  • 38
    • 0037864281 scopus 로고    scopus 로고
    • Repair of UV damage in Halobacterium salinarum
    • McCready S, Marcello L (2003) Repair of UV damage in Halobacterium salinarum. Biochem Soc Trans 31:694-698
    • (2003) Biochem Soc Trans , vol.31 , pp. 694-698
    • McCready, S.1    Marcello, L.2
  • 40
    • 0001376922 scopus 로고
    • The enzymatic synthesis of riboflavin
    • Plaut GWE, Harvey RA (1971) The enzymatic synthesis of riboflavin. Methods Enzymol 18B:515-538
    • (1971) Methods Enzymol , vol.18 B , pp. 515-538
    • Plaut, G.W.E.1    Harvey, R.A.2
  • 42
    • 0012023519 scopus 로고    scopus 로고
    • Characterization of a bifunctional enzyme fusion of trehalose-6- phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli
    • Seo HS, Koo YJ, Lim JY, Song JT, Kim CH, Kim JK, Lee JS, Choi YD (2000) Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli. Appl Environ Microbiol 66:2484-2490
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2484-2490
    • Seo, H.S.1    Koo, Y.J.2    Lim, J.Y.3    Song, J.T.4    Kim, C.H.5    Kim, J.K.6    Lee, J.S.7    Choi, Y.D.8
  • 44
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29: 1097-1106
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 45
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S, Richardson CC (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci USA 82:1074-1078
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 46
    • 0000396592 scopus 로고
    • Pyrimidopteridines by oxidative self-condensation of aminopyrimidines
    • Taylor EC, Jr., Loux HM, Falco E, Hitchings GH (1955) Pyrimidopteridines by oxidative self-condensation of aminopyrimidines. J Am Chem Soc 77:2243-2248
    • (1955) J Am Chem Soc , vol.77 , pp. 2243-2248
    • Taylor Jr., E.C.1    Loux, H.M.2    Falco, E.3    Hitchings, G.H.4
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 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


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