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Volumn 53, Issue 28, 2014, Pages 4635-4647

Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of methanofuran

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CYTOLOGY; GALLIUM; GENES; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METHANOL;

EID: 84904612226     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500615p     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 0033005876 scopus 로고    scopus 로고
    • Enzymology of one-carbon metabolism in methanogenic pathways
    • Ferry, J. G. (1999) Enzymology of one-carbon metabolism in methanogenic pathways FEMS Microbiol. Rev. 23, 13-38
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 13-38
    • Ferry, J.G.1
  • 3
    • 0021441677 scopus 로고
    • Structure of Methanofuran, the Carbon-Dioxide Reduction Factor of Methanobacterium thermoautotrophicum
    • Leigh, J. A., Rinehart, K. L., and Wolfe, R. S. (1984) Structure of Methanofuran, the Carbon-Dioxide Reduction Factor of Methanobacterium thermoautotrophicum J. Am. Chem. Soc. 106, 3636-3640
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3636-3640
    • Leigh, J.A.1    Rinehart, K.L.2    Wolfe, R.S.3
  • 4
    • 0000272797 scopus 로고
    • Methane emissions from rice fields
    • Neue, H. (1993) Methane emissions from rice fields BioScience 43, 466-476
    • (1993) BioScience , vol.43 , pp. 466-476
    • Neue, H.1
  • 5
    • 14544282848 scopus 로고    scopus 로고
    • Identification and characterization of a l -tyrosine decarboxylase in Methanocaldococcus jannaschii
    • Kezmarsky, N. D., Xu, H., Graham, D. E., and White, R. H. (2005) Identification and characterization of a l -tyrosine decarboxylase in Methanocaldococcus jannaschii Biochim. Biophys. Acta 1722, 175-182
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 175-182
    • Kezmarsky, N.D.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 6
    • 0024095484 scopus 로고
    • Structural Diversity among Methanofurans from Different Methanogenic Bacteria
    • White, R. H. (1988) Structural Diversity among Methanofurans from Different Methanogenic Bacteria J. Bacteriol. 170, 4594-4597
    • (1988) J. Bacteriol. , vol.170 , pp. 4594-4597
    • White, R.H.1
  • 7
    • 84875251958 scopus 로고    scopus 로고
    • Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis
    • Sarmiento, F., Mrazek, J., and Whitman, W. B. (2013) Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis Proc. Natl. Acad. Sci. U.S.A. 110, 4726-4731
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4726-4731
    • Sarmiento, F.1    Mrazek, J.2    Whitman, W.B.3
  • 8
    • 0027534777 scopus 로고
    • Metabolic Pathways in Methanococcus jannaschii and Other Methanogenic Bacteria
    • Sprott, G. D., Ekiel, I., and Patel, G. B. (1993) Metabolic Pathways in Methanococcus jannaschii and Other Methanogenic Bacteria Appl. Environ. Microbiol. 59, 1092-1098
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1092-1098
    • Sprott, G.D.1    Ekiel, I.2    Patel, G.B.3
  • 10
    • 0023333624 scopus 로고
    • Structure of a methanofuran derivative found in cell extracts of Methanosarcina barkeri
    • Bobik, T. A., Donnelly, M. I., Rinehart, K. L., Jr., and Wolfe, R. S. (1987) Structure of a methanofuran derivative found in cell extracts of Methanosarcina barkeri Arch. Biochem. Biophys. 254, 430-436
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 430-436
    • Bobik, T.A.1    Donnelly, M.I.2    Rinehart, Jr.K.L.3    Wolfe, R.S.4
  • 11
    • 0028277466 scopus 로고
    • Availability of Fluorogenic Reagents Having a Benzofurazan Structure in the Biosciences
    • Imai, K., Uzu, S., Kanda, S., and Baeyens, W. R. G. (1994) Availability of Fluorogenic Reagents Having a Benzofurazan Structure in the Biosciences Anal. Chim. Acta 290, 3-20
    • (1994) Anal. Chim. Acta , vol.290 , pp. 3-20
    • Imai, K.1    Uzu, S.2    Kanda, S.3    Baeyens, W.R.G.4
  • 12
    • 9344268649 scopus 로고
    • Biosynthesis of the 1,3,4,6-Hexanetetracarboxylic Acid Subunit of Methanofuran
    • White, R. H. (1987) Biosynthesis of the 1,3,4,6-Hexanetetracarboxylic Acid Subunit of Methanofuran Biochemistry 26, 3163-3167
    • (1987) Biochemistry , vol.26 , pp. 3163-3167
    • White, R.H.1
  • 13
    • 0024286080 scopus 로고
    • Biosynthesis of the 2-(aminomethyl)-4-(hydroxymethyl)furan subunit of methanofuran
    • White, R. H. (1988) Biosynthesis of the 2-(aminomethyl)-4-(hydroxymethyl) furan subunit of methanofuran Biochemistry 27, 4415-4420
    • (1988) Biochemistry , vol.27 , pp. 4415-4420
    • White, R.H.1
  • 14
    • 0026657154 scopus 로고
    • Biosynthesis of methanofuran in Methanobacterium thermoautotrophicum
    • Eisenreich, W. and Bacher, A. (1992) Biosynthesis of methanofuran in Methanobacterium thermoautotrophicum J. Biol. Chem. 267, 17574-17580
    • (1992) J. Biol. Chem. , vol.267 , pp. 17574-17580
    • Eisenreich, W.1    Bacher, A.2
  • 16
    • 4544325884 scopus 로고
    • Vanillic Acid
    • (Rabjohn, N. Ed.) pp, Wiley, New York
    • Pearl, I. A. (1963) Vanillic Acid. In Organic Synthesis (Rabjohn, N., Ed.) pp 972-976, Wiley, New York.
    • (1963) Organic Synthesis , pp. 972-976
    • Pearl, I.A.1
  • 17
    • 42449141472 scopus 로고    scopus 로고
    • Biochemical origins of lactaldehyde and hydroxyacetone in Methanocaldococcus jannaschii
    • White, R. H. (2008) Biochemical origins of lactaldehyde and hydroxyacetone in Methanocaldococcus jannaschii Biochemistry 47, 5037-5046
    • (2008) Biochemistry , vol.47 , pp. 5037-5046
    • White, R.H.1
  • 18
    • 69449096273 scopus 로고    scopus 로고
    • Aminoacetone as the penultimate precursor to the antitumor agent azinomycin A
    • Sharma, V., Kelly, G. T., Foulke-Abel, J., and Watanabe, C. M. (2009) Aminoacetone as the penultimate precursor to the antitumor agent azinomycin A Org. Lett. 11, 4006-4009
    • (2009) Org. Lett. , vol.11 , pp. 4006-4009
    • Sharma, V.1    Kelly, G.T.2    Foulke-Abel, J.3    Watanabe, C.M.4
  • 19
    • 33749509235 scopus 로고    scopus 로고
    • Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: A precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii
    • White, R. H. and Xu, H. (2006) Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: A precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii Biochemistry 45, 12366-12379
    • (2006) Biochemistry , vol.45 , pp. 12366-12379
    • White, R.H.1    Xu, H.2
  • 21
    • 34247624668 scopus 로고    scopus 로고
    • Synthesis and characterization of a new fluorescent probe for reactive oxygen species
    • Heyne, B., Beddie, C., and Scaiano, J. C. (2007) Synthesis and characterization of a new fluorescent probe for reactive oxygen species Org. Biomol. Chem. 5, 1454-1458
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 1454-1458
    • Heyne, B.1    Beddie, C.2    Scaiano, J.C.3
  • 22
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. and Van Aalten, D. M. (2004) PRODRG: A tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr. D60, 1355-1363
    • (2004) Acta Crystallogr. , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 23
    • 38949211854 scopus 로고    scopus 로고
    • Crystal Structure of MJ0684 from Methanococcus jannaschii, a Novel Archaeal Homolog of Kynurenine Aminotransferase
    • Yang, J. K. (2008) Crystal Structure of MJ0684 from Methanococcus jannaschii, a Novel Archaeal Homolog of Kynurenine Aminotransferase Bull. Korean Chem. Soc. 29, 173-176
    • (2008) Bull. Korean Chem. Soc. , vol.29 , pp. 173-176
    • Yang, J.K.1
  • 25
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the Speed and Accuracy of Docking with a New Scoring Function, Efficient Optimization, and Multithreading
    • Trott, O. and Olson, A. J. (2010) AutoDock Vina: Improving the Speed and Accuracy of Docking with a New Scoring Function, Efficient Optimization, and Multithreading J. Comput. Chem. 31, 455-461
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 26
    • 0021200154 scopus 로고
    • Rapidly growing rumen methanogenic organism that synthesizes coenzyme M and has a high affinity for formate
    • Lovley, D. R., Greening, R. C., and Ferry, J. G. (1984) Rapidly growing rumen methanogenic organism that synthesizes coenzyme M and has a high affinity for formate Appl. Environ. Microbiol. 48, 81-87
    • (1984) Appl. Environ. Microbiol. , vol.48 , pp. 81-87
    • Lovley, D.R.1    Greening, R.C.2    Ferry, J.G.3
  • 28
    • 0032479058 scopus 로고    scopus 로고
    • C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea
    • Chistoserdova, L., Vorholt, J. A., Thauer, R. K., and Lidstrom, M. E. (1998) C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea Science 281, 99-102
    • (1998) Science , vol.281 , pp. 99-102
    • Chistoserdova, L.1    Vorholt, J.A.2    Thauer, R.K.3    Lidstrom, M.E.4
  • 29
    • 0035725851 scopus 로고    scopus 로고
    • Characterization of the formyltransferase from Methylobacterium extorquens AM1
    • Pomper, B. K. and Vorholt, J. A. (2001) Characterization of the formyltransferase from Methylobacterium extorquens AM1 Eur. J. Biochem. 268, 4769-4775
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4769-4775
    • Pomper, B.K.1    Vorholt, J.A.2
  • 30
    • 0027286747 scopus 로고
    • Mechanism for the formation of methylglyoxal from triosephosphates
    • Richard, J. P. (1993) Mechanism for the formation of methylglyoxal from triosephosphates Biochem. Soc. Trans. 21, 549-553
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 549-553
    • Richard, J.P.1
  • 31
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates: Investigation using a specific assay for methylglyoxal
    • Phillips, S. A. and Thornalley, P. J. (1993) The formation of methylglyoxal from triose phosphates: Investigation using a specific assay for methylglyoxal Eur. J. Biochem. 212, 101-105
    • (1993) Eur. J. Biochem. , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 32
    • 0034696583 scopus 로고    scopus 로고
    • Mirroring perfection: The structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate
    • Saadat, D. and Harrison, D. H. (2000) Mirroring perfection: The structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate Biochemistry 39, 2950-2960
    • (2000) Biochemistry , vol.39 , pp. 2950-2960
    • Saadat, D.1    Harrison, D.H.2
  • 33
    • 0037348392 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii
    • Yang, J. K., Chang, C. S., Cho, S. J., Lee, J. Y., Yu, Y. G., Eom, S. H., and Suh, S. W. (2003) Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii Acta Crystallogr. 59, 563-565
    • (2003) Acta Crystallogr. , vol.59 , pp. 563-565
    • Yang, J.K.1    Chang, C.S.2    Cho, S.J.3    Lee, J.Y.4    Yu, Y.G.5    Eom, S.H.6    Suh, S.W.7
  • 34
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani, R. and Peracchi, A. (2003) A genomic overview of pyridoxal-phosphate-dependent enzymes EMBO Rep. 4, 850-854
    • (2003) EMBO Rep. , vol.4 , pp. 850-854
    • Percudani, R.1    Peracchi, A.2
  • 35
    • 0032537603 scopus 로고    scopus 로고
    • The catalytic mechanism of kynureninase from Pseudomonas fluorescens: Evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry
    • Phillips, R. S., Sundararaju, B., and Koushik, S. V. (1998) The catalytic mechanism of kynureninase from Pseudomonas fluorescens: Evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry Biochemistry 37, 8783-8789
    • (1998) Biochemistry , vol.37 , pp. 8783-8789
    • Phillips, R.S.1    Sundararaju, B.2    Koushik, S.V.3
  • 36
    • 70349132705 scopus 로고    scopus 로고
    • Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: Enzymes and genes in a patchwork pathway
    • Mayer, J. and Cook, A. M. (2009) Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: Enzymes and genes in a patchwork pathway J. Bacteriol. 191, 6052-6058
    • (2009) J. Bacteriol. , vol.191 , pp. 6052-6058
    • Mayer, J.1    Cook, A.M.2
  • 37
    • 4644248835 scopus 로고    scopus 로고
    • Crystal structures of unbound and aminooxyacetate-bound Escherichia coli γ-aminobutyrate aminotransferase
    • Liu, W., Peterson, P. E., Carter, R. J., Zhou, X., Langston, J. A., Fisher, A. J., and Toney, M. D. (2004) Crystal structures of unbound and aminooxyacetate-bound Escherichia coli γ-aminobutyrate aminotransferase Biochemistry 43, 10896-10905
    • (2004) Biochemistry , vol.43 , pp. 10896-10905
    • Liu, W.1    Peterson, P.E.2    Carter, R.J.3    Zhou, X.4    Langston, J.A.5    Fisher, A.J.6    Toney, M.D.7
  • 38
    • 0017904470 scopus 로고
    • 2-acetylornithine 5-aminotransferase of Klebsiella aerogenes: Control of synthesis by induction, catabolite repression, and activation by glutamine synthetase
    • 2-acetylornithine 5-aminotransferase of Klebsiella aerogenes: Control of synthesis by induction, catabolite repression, and activation by glutamine synthetase J. Bacteriol. 133, 686-691
    • (1978) J. Bacteriol. , vol.133 , pp. 686-691
    • Friedrich, B.1    Friedrich, C.G.2    Magasanik, B.3
  • 39
    • 24644442264 scopus 로고    scopus 로고
    • Dual Substrate Recognition of Aminotransferases
    • Hirotsu, K., Goto, M., Okamoto, A., and Miyahara, I. (2005) Dual Substrate Recognition of Aminotransferases Chem. Rec. 5, 160-172
    • (2005) Chem. Rec. , vol.5 , pp. 160-172
    • Hirotsu, K.1    Goto, M.2    Okamoto, A.3    Miyahara, I.4
  • 40
    • 84893744859 scopus 로고    scopus 로고
    • Aspartate aminotransferase: An old dog teaches new tricks
    • Toney, M. D. (2014) Aspartate aminotransferase: An old dog teaches new tricks Arch. Biochem. Biophys. 544, 119-127
    • (2014) Arch. Biochem. Biophys. , vol.544 , pp. 119-127
    • Toney, M.D.1
  • 42
    • 0021847757 scopus 로고
    • Evidence of a common pathway of carbon dioxide reduction to methane in methanogens
    • Jones, W. J., Donnelly, M. I., and Wolfe, R. S. (1985) Evidence of a common pathway of carbon dioxide reduction to methane in methanogens J. Bacteriol. 163, 126-131
    • (1985) J. Bacteriol. , vol.163 , pp. 126-131
    • Jones, W.J.1    Donnelly, M.I.2    Wolfe, R.S.3
  • 43
    • 0017709116 scopus 로고
    • Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum
    • Zeikus, J. G., Fuchs, G., Kenealy, W., and Thauer, R. K. (1977) Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum J. Bacteriol. 132, 604-613
    • (1977) J. Bacteriol. , vol.132 , pp. 604-613
    • Zeikus, J.G.1    Fuchs, G.2    Kenealy, W.3    Thauer, R.K.4
  • 44
    • 0024671797 scopus 로고
    • A novel biosynthesis of medium chain length α-ketodicarboxylic acids in methanogenic archaebacteria
    • White, R. H. (1989) A novel biosynthesis of medium chain length α-ketodicarboxylic acids in methanogenic archaebacteria Arch. Biochem. Biophys. 270, 691-697
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 691-697
    • White, R.H.1
  • 46
    • 0032564596 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-Amino-5-hydroxymethyl-2- methylpyrimidine kinase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase
    • Reddick, J. J., Kinsland, C., Nicewonger, R., Christian, T., Downs, D. M., Winkler, M. E., and Begley, T. P. (1998) Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-Amino-5-hydroxymethyl-2-methylpyrimidine kinase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase Tetrahedron 54, 15983-15991
    • (1998) Tetrahedron , vol.54 , pp. 15983-15991
    • Reddick, J.J.1    Kinsland, C.2    Nicewonger, R.3    Christian, T.4    Downs, D.M.5    Winkler, M.E.6    Begley, T.P.7
  • 48
    • 0029923835 scopus 로고    scopus 로고
    • Biosynthesis of methanopterin
    • White, R. H. (1996) Biosynthesis of methanopterin Biochemistry 35, 3447-3456
    • (1996) Biochemistry , vol.35 , pp. 3447-3456
    • White, R.H.1
  • 49
    • 84869388277 scopus 로고    scopus 로고
    • Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate
    • Crecy-Lagard, V., Phillips, G., Grochowski, L. L., Yacoubi, B. E., Jenney, F., Adams, M. W., Murzin, A. G., and White, R. H. (2012) Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate ACS Chem. Biol. 7, 1807-1816
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1807-1816
    • Crecy-Lagard, V.1    Phillips, G.2    Grochowski, L.L.3    Yacoubi, B.E.4    Jenney, F.5    Adams, M.W.6    Murzin, A.G.7    White, R.H.8


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