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Volumn 249, Issue 1, 1997, Pages 280-285

Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction

Author keywords

Coenzyme M; Corrinoid enzyme; Methanogenesis from methanol; Methyltransferase; Zinc enzyme

Indexed keywords

METHYLTRANSFERASE;

EID: 0030879503     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00280.x     Document Type: Article
Times cited : (77)

References (22)
  • 1
    • 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
  • 2
    • 0029787826 scopus 로고    scopus 로고
    • Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
    • Daas, P. J. H., Hagen, W. R., Keltjens, J. T., van der Drift, C. & Vogels, G. D. (1996) Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri, J. Biol. Chem. 271, 22 346-22 351.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22346-22351
    • Daas, P.J.H.1    Hagen, W.R.2    Keltjens, J.T.3    Van Der Drift, C.4    Vogels, G.D.5
  • 4
    • 14444276994 scopus 로고    scopus 로고
    • Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri
    • Ferguson, D. J. Jr & Krzycki, J. A. (1997) Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri, J. Bacteriol. 179, 846-852.
    • (1997) J. Bacteriol. , vol.179 , pp. 846-852
    • Ferguson Jr., D.J.1    Krzycki, J.A.2
  • 5
    • 0029760593 scopus 로고    scopus 로고
    • Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme
    • Gonzalez, J. C., Peariso, K., Penner-Hahn, J. E. & Matthews, R. G. (1996) Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme, Biochemistry 35, 12 228-12 234.
    • (1996) Biochemistry , vol.35 , pp. 12228-12234
    • Gonzalez, J.C.1    Peariso, K.2    Penner-Hahn, J.E.3    Matthews, R.G.4
  • 6
    • 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. & 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
  • 7
    • 0024962345 scopus 로고
    • Different isozymes of methylcobalamin:2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri
    • Grahame, D. A. (1989) Different isozymes of methylcobalamin:2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri, J. Biol. Chem. 264, 12 890-12 894.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12890-12894
    • Grahame, D.A.1
  • 8
    • 0029671414 scopus 로고    scopus 로고
    • Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli
    • Harms, U. & Thauer, R. K. (1996a) Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli, Eur. J. Biochem. 235, 653-659.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 653-659
    • Harms, U.1    Thauer, R.K.2
  • 9
    • 0029846834 scopus 로고    scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum. EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum. EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide, Eur. J. Biochem. 241, 149-154.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 149-154
    • Harms, U.1    Thauer, R.K.2
  • 10
    • 0001780722 scopus 로고
    • Conversion of methanol and methylamines to methane and carbon dioxide
    • Ferry, J. G., ed. Chapman & Hall, New York
    • Keltjens, J. T. & Vogels, G. D. (1993) Conversion of methanol and methylamines to methane and carbon dioxide, in Methanogenesis (Ferry, J. G., ed.) pp. 253-303, Chapman & Hall, New York.
    • (1993) Methanogenesis , pp. 253-303
    • Keltjens, J.T.1    Vogels, G.D.2
  • 11
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression
    • LeClerc, G. M. & Grahame, D. A. (1996) Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression, J. Biol. Chem. 271, 18 725-18 731.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 13
    • 0001029771 scopus 로고
    • Providing one-carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase
    • Matthews, R. G. & Drummond, J. T. (1990) Providing one-carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase, Chem. Rev. 90, 1275-1290.
    • (1990) Chem. Rev. , vol.90 , pp. 1275-1290
    • Matthews, R.G.1    Drummond, J.T.2
  • 14
    • 0022019307 scopus 로고
    • Metal binding to yeast aminopeptidase 1
    • Röhm, K.-H. (1985) Metal binding to yeast aminopeptidase 1, Eur. J. Biochem. 146, 633-639.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 633-639
    • Röhm, K.-H.1
  • 15
    • 0031024751 scopus 로고    scopus 로고
    • Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1
    • Sauer, K., Harms, U. & Thauer, R. K. (1997) Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1, Eur. J. Biochem. 243, 670-677.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 670-677
    • Sauer, K.1    Harms, U.2    Thauer, R.K.3
  • 16
    • 0029935034 scopus 로고    scopus 로고
    • Coenzyme M methylase activity of the 480-kilodalton corrinoid protein from Methanosarcina barkeri
    • Tallant, T. C. & Krzycki, J. A. (1996) Coenzyme M methylase activity of the 480-kilodalton corrinoid protein from Methanosarcina barkeri, J. Bacteriol. 175, 1295-1301.
    • (1996) J. Bacteriol. , vol.175 , pp. 1295-1301
    • Tallant, T.C.1    Krzycki, J.A.2
  • 18
    • 0021066544 scopus 로고
    • Involvement of corrinoids in the methylation of coenzyme M (2-mercaptoethanesulfonic acid) by methanol and enzymes from Methanosarcina barkeri
    • van der Meijden, P., Jansen, L. P. J. M., van der Drift, C. & Vogels, G. D. (1983b) Involvement of corrinoids in the methylation of coenzyme M (2-mercaptoethanesulfonic acid) by methanol and enzymes from Methanosarcina barkeri, FEMS Microbiol. Lett. 19, 247-251.
    • (1983) FEMS Microbiol. Lett. , vol.19 , pp. 247-251
    • Meijden, P.1    Jansen, L.P.J.M.2    Van Der Drift, C.3    Vogels, G.D.4
  • 19
    • 0028587832 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor, Eur. J. Biochem. 226, 799-809.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 799-809
    • Weiss, D.S.1    Gärtner, P.2    Thauer, R.K.3
  • 20
    • 0028994310 scopus 로고
    • Thermostable amino-acylase from Bacillus stearothermophilus: Significance of the metal center for catalysis and protein stability
    • Weiß, H. M. Palm, G. J. & Röhm, K.-H. (1995) Thermostable amino-acylase from Bacillus stearothermophilus: significance of the metal center for catalysis and protein stability, Biol. Chem. Hoppe-Seyler 376, 643-649.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 643-649
    • Weiß, H.M.1    Palm, G.J.2    Röhm, K.-H.3
  • 21
    • 0017036833 scopus 로고
    • Titanium(III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes
    • Zehnder, A. J. B. & Wuhrmann, K. (1976) Titanium(III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes, Science 194, 1165-1166.
    • (1976) Science , vol.194 , pp. 1165-1166
    • Zehnder, A.J.B.1    Wuhrmann, K.2
  • 22
    • 0028846885 scopus 로고
    • Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: Origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein
    • Zhao, S., Roberts, D. L. & Ragsdale, S. W. (1995) Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein, Biochemistry 34, 15 075-15 083.
    • (1995) Biochemistry , vol.34 , pp. 15075-15083
    • Zhao, S.1    Roberts, D.L.2    Ragsdale, S.W.3


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