메뉴 건너뛰기




Volumn 284, Issue 39, 2009, Pages 26217-26228

A love affair with vitamins

Author keywords

[No Author keywords available]

Indexed keywords

5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); DIHYDROLIPOAMIDE DEHYDROGENASE; FLAVOPROTEIN; G PROTEIN COUPLED RECEPTOR; GLUTATHIONE REDUCTASE; HISTIDINE; MECOBALAMIN; METHIONINE SYNTHASE; OXIDOREDUCTASE; QUERCETIN; RETINOL; RHODOPSIN; RIBOFLAVIN; TETRAHYDROFOLIC ACID; VANILLIN;

EID: 70350353513     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.X109.041178     Document Type: Article
Times cited : (4)

References (40)
  • 2
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, I., and Changeux, J. P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, I.2    Changeux, J.P.3
  • 3
    • 0014669713 scopus 로고
    • The isolation of old yellow enzyme in free and complexed forms
    • Matthews, R. G., and Massey, V. (1969) The isolation of old yellow enzyme in free and complexed forms. J. Biol Chem. 244, 1779-1786
    • (1969) J. Biol Chem , vol.244 , pp. 1779-1786
    • Matthews, R.G.1    Massey, V.2
  • 4
    • 0016766271 scopus 로고
    • Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme
    • Matthews, R. G., Massey, V., and Sweeley, C. C. (1975) Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. J. Biol. Chem. 250, 9294-9298
    • (1975) J. Biol. Chem , vol.250 , pp. 9294-9298
    • Matthews, R.G.1    Massey, V.2    Sweeley, C.C.3
  • 5
    • 0017082516 scopus 로고
    • Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart
    • Matthews, R. G., and Williams, C. H., Jr. (1976) Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. J. Biol. Chem. 251, 3956-3964
    • (1976) J. Biol. Chem , vol.251 , pp. 3956-3964
    • Matthews, R.G.1    Williams Jr., C.H.2
  • 7
    • 0015228022 scopus 로고
    • Mammalian methylenetetrahydrofolate reductase: Partial purification, properties, and inhibition by S-adenosylmethionine
    • Kutzbach, C., and Stokstad, E. L. (1971) Mammalian methylenetetrahydrofolate reductase: partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta 250, 459-477
    • (1971) Biochim. Biophys. Acta , vol.250 , pp. 459-477
    • Kutzbach, C.1    Stokstad, E.L.2
  • 8
    • 53049090543 scopus 로고    scopus 로고
    • 12 coenzyme and the role of the vitamin in methionine synthesis
    • 12 coenzyme and the role of the vitamin in methionine synthesis. J. Biol. Chem. 283, 23497-23504
    • (2008) J. Biol. Chem , vol.283 , pp. 23497-23504
    • Weissbach, H.1
  • 9
    • 0016173119 scopus 로고
    • Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system
    • Fujii, K., and Huennekens, F. M. (1974) Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system. J. Biol. Chem. 249, 6745-6753
    • (1974) J. Biol. Chem , vol.249 , pp. 6745-6753
    • Fujii, K.1    Huennekens, F.M.2
  • 10
    • 0008336988 scopus 로고
    • Cofactor requirements and intermediates in methionine biosynthesis
    • Mangum, J. H., and Scrimgeour, K. G. (1962) Cofactor requirements and intermediates in methionine biosynthesis. Fed. Proc. 21, 242
    • (1962) Fed. Proc , vol.21 , pp. 242
    • Mangum, J.H.1    Scrimgeour, K.G.2
  • 11
    • 0034047840 scopus 로고    scopus 로고
    • Ten commandments: Lessons from the enzymology of DNA replication
    • Kornberg, A. (2000) Ten commandments: lessons from the enzymology of DNA replication. J. Bacteriol. 182, 3613-3618
    • (2000) J. Bacteriol , vol.182 , pp. 3613-3618
    • Kornberg, A.1
  • 12
    • 0020478526 scopus 로고
    • Purification and properties of methylenetetrahydrofolate reductase from pig liver
    • Daubner, S. C., and Matthews, R. G. (1982) Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem. 257, 140-145
    • (1982) J. Biol. Chem , vol.257 , pp. 140-145
    • Daubner, S.C.1    Matthews, R.G.2
  • 13
    • 0035909980 scopus 로고    scopus 로고
    • Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase
    • Yamada, K., Chen, Z., Rozen, R., and Matthews, R. G. (2001) Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. Proc. Nat. Acad. Sci. U.S.A. 98, 14853-14858
    • (2001) Proc. Nat. Acad. Sci. U.S.A , vol.98 , pp. 14853-14858
    • Yamada, K.1    Chen, Z.2    Rozen, R.3    Matthews, R.G.4
  • 14
    • 62149148038 scopus 로고    scopus 로고
    • Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex
    • Wolthers, K. R., and Scrutton, N.S. (2009) Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex. FEBS J. 276, 1942-1951
    • (2009) FEBS J , vol.276 , pp. 1942-1951
    • Wolthers, K.R.1    Scrutton, N.S.2
  • 15
    • 0028487161 scopus 로고
    • Human methylenetetrahydrofolate reductase: Isolation of cDNA, mapping and mutation identification
    • Goyette, P., Sumner, J. S., Milos, R., Duncan, A. M., Rosenblatt, D. S., Matthews, R. G., and Rozen, R. (1994) Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nat. Genet. 7, 195-200
    • (1994) Nat. Genet , vol.7 , pp. 195-200
    • Goyette, P.1    Sumner, J.S.2    Milos, R.3    Duncan, A.M.4    Rosenblatt, D.S.5    Matthews, R.G.6    Rozen, R.7
  • 16
    • 0026034240 scopus 로고
    • Thermolabile methylenetetrahydrofolate reductase: An inherited risk factor for coronary artery disease
    • Kang, S. S., Wong P. W., Susmano, A., Sora, J., Norusis, M, and Ruggie, N. (1991) Thermolabile methylenetetrahydrofolate reductase: an inherited risk factor for coronary artery disease. Am. J. Hum. Genet. 48, 536-545
    • (1991) Am. J. Hum. Genet , vol.48 , pp. 536-545
    • Kang, S.S.1    Wong, P.W.2    Susmano, A.3    Sora, J.4    Norusis, M.5    Ruggie, N.6
  • 18
    • 0032945180 scopus 로고    scopus 로고
    • Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli
    • Sheppard, C. A., Trimmer, E. E., and Matthews, R. G. (1999) Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli. J. Bacteriol. 181, 718-725
    • (1999) J. Bacteriol , vol.181 , pp. 718-725
    • Sheppard, C.A.1    Trimmer, E.E.2    Matthews, R.G.3
  • 19
    • 0032895522 scopus 로고    scopus 로고
    • The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia
    • Guenther, B. D., Sheppard, C. A., Tran, P., Rozen, R., Matthews, R. G., and Ludwig, M. L. (1999) The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 6, 359-365
    • (1999) Nat. Struct. Biol , vol.6 , pp. 359-365
    • Guenther, B.D.1    Sheppard, C.A.2    Tran, P.3    Rozen, R.4    Matthews, R.G.5    Ludwig, M.L.6
  • 20
    • 23044461104 scopus 로고    scopus 로고
    • Regulation of human methylenetetrahydrofolate reductase by phosphorylation
    • Yamada, K., Strahler, J. R., Andrews, P. C., and Matthews, R. G. (2005) Regulation of human methylenetetrahydrofolate reductase by phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 102, 10454-10459
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 10454-10459
    • Yamada, K.1    Strahler, J.R.2    Andrews, P.C.3    Matthews, R.G.4
  • 21
    • 0027310848 scopus 로고
    • The effects of phosphorylation on the structure and function of proteins
    • Johnson, L. N., and Barford, D. (1993) The effects of phosphorylation on the structure and function of proteins, Annu. Rev. Biophys. Biomol. Struct. 22, 199-232
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 199-232
    • Johnson, L.N.1    Barford, D.2
  • 22
    • 0024364303 scopus 로고
    • Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain
    • Banerjee, R. V., Johnston, N. Sobeski, J. K., Datta, P., and Matthews, R. G. (1989) Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264, 13888-13895
    • (1989) J. Biol. Chem , vol.264 , pp. 13888-13895
    • Banerjee, R.V.1    Johnston, N.2    Sobeski, J.K.3    Datta, P.4    Matthews, R.G.5
  • 23
    • 0022259920 scopus 로고
    • The LDL receptor gene: A mosaic of exons shared with different proteins
    • Südhof, T. C., Goldstein, J. L., Brown, M. S., and Russell, D. W. (1985) The LDL receptor gene: a mosaic of exons shared with different proteins. Science 228, 815-822
    • (1985) Science , vol.228 , pp. 815-822
    • Südhof, T.C.1    Goldstein, J.L.2    Brown, M.S.3    Russell, D.W.4
  • 24
    • 0030829339 scopus 로고    scopus 로고
    • Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine
    • Goulding, C. W., Postigo, D., and Matthews, R. G. (1997) Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry 36, 8082-8091
    • (1997) Biochemistry , vol.36 , pp. 8082-8091
    • Goulding, C.W.1    Postigo, D.2    Matthews, R.G.3
  • 26
    • 0026776985 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli
    • Luschinsky, C. L., Drummond, J. T., Matthews, R. G., and Ludwig, M. L. (1992) Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. J. Mol. Biol. 225, 557-560
    • (1992) J. Mol. Biol , vol.225 , pp. 557-560
    • Luschinsky, C.L.1    Drummond, J.T.2    Matthews, R.G.3    Ludwig, M.L.4
  • 28
    • 0026701740 scopus 로고
    • Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes
    • Marsh, E. N., and Holloway, D. E. (1992) Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes, FEBS Lett. 310, 167-170
    • (1992) FEBS Lett , vol.310 , pp. 167-170
    • Marsh, E.N.1    Holloway, D.E.2
  • 30
    • 0031012260 scopus 로고    scopus 로고
    • Interaction of Escherichia coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: Binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor
    • Hoover, D. M., Jarrett, J. T., Sands, R. H., Dunham, W. R., Ludwig, M. L., and Matthews, R. G. (1997) Interaction of Escherichia coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor. Biochemistry 36, 127-138
    • (1997) Biochemistry , vol.36 , pp. 127-138
    • Hoover, D.M.1    Jarrett, J.T.2    Sands, R.H.3    Dunham, W.R.4    Ludwig, M.L.5    Matthews, R.G.6
  • 34
    • 0038154035 scopus 로고    scopus 로고
    • Factors modulating conformational equilibria in large modular proteins: A case study with cobalamin-dependent methionine synthase
    • Bandarian, V., Ludwig, M. L., and Matthews, R. G. (2003) Factors modulating conformational equilibria in large modular proteins: a case study with cobalamin-dependent methionine synthase. Proc. Natl. Acad. Sci. U.S.A. 100, 8156-8163
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 8156-8163
    • Bandarian, V.1    Ludwig, M.L.2    Matthews, R.G.3
  • 35
    • 41949094246 scopus 로고    scopus 로고
    • A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor
    • Datta, S., Koutmos, M., Pattridge, K. A., Ludwig, M. L., and Matthews, R. G. (2008) A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor. Proc. Natl. Acad. Sci. U.S.A. 105, 4115-4120
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 4115-4120
    • Datta, S.1    Koutmos, M.2    Pattridge, K.A.3    Ludwig, M.L.4    Matthews, R.G.5
  • 36
    • 0000362963 scopus 로고
    • 13C in the organic ligand and the thermodynamics of the base-on/base-off reaction
    • 13C in the organic ligand and the thermodynamics of the base-on/base-off reaction. Inorg. Chem. 27, 3548-3555
    • (1988) Inorg. Chem , vol.27 , pp. 3548-3555
    • Brown, K.L.1    Peck-Siler, S.2
  • 37
    • 35648996376 scopus 로고    scopus 로고
    • The ligand trans influence governs conformation in cobalamin-dependent methionine synthase
    • Fleischhacker, A. S., and Matthews, R. G. (2007) The ligand trans influence governs conformation in cobalamin-dependent methionine synthase. Biochemistry 46, 12382-12392
    • (2007) Biochemistry , vol.46 , pp. 12382-12392
    • Fleischhacker, A.S.1    Matthews, R.G.2
  • 38
    • 70350422422 scopus 로고    scopus 로고
    • Corrinoid- and cobalamin-dependent methyltransferases
    • Sigal, A, Sigal, H, and Sigal, R. K. O, eds Royal Society of Chemistry, London, in press
    • Matthews, R. G. (2009) Corrinoid- and cobalamin-dependent methyltransferases. In: Metal Ions in Life Sciences: Metal-Carbon Bonds in Enzymes and Cofactors (Sigal, A., Sigal, H., and Sigal, R. K. O., eds) Vol. 6, Royal Society of Chemistry, London, in press
    • (2009) Metal Ions in Life Sciences: Metal-Carbon Bonds in Enzymes and Cofactors , vol.6
    • Matthews, R.G.1
  • 39
    • 33846809521 scopus 로고    scopus 로고
    • Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex
    • Hagemeier, C. H., Krer, M., Thauer, R. K., Warkentin, B., and Ermler, U. (2006) Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex. Proc. Natl. Acad. Sci. U.S.A. 103, 18917-18922
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18917-18922
    • Hagemeier, C.H.1    Krer, M.2    Thauer, R.K.3    Warkentin, B.4    Ermler, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.