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Volumn 261, Issue 3, 1999, Pages 674-681

Methanol:coenzyme M methyltransferase from Methanosarcina barkeri - Substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin

Author keywords

Cobalamin; Cobinamide; Coenzyme M; Methane formation; Methanogenic archaea; Methanosarcina barkeri; Methyltransferase

Indexed keywords

COBALAMIN; COBINAMIDE; CORRINOID; IMIDAZOLE DERIVATIVE; MECOBALAMIN; METHANOL; METHIONINE SYNTHASE; METHYLTRANSFERASE; POLYPEPTIDE;

EID: 0033135588     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00355.x     Document Type: Article
Times cited : (38)

References (38)
  • 1
    • 0018831899 scopus 로고
    • 1 compounds by Methanosarcina barkeri
    • 1 compounds by Methanosarcina barkeri. J. Bacteriol. 141, 728-734.
    • (1980) J. Bacteriol. , vol.141 , pp. 728-734
    • Shapiro, S.1    Wolfe, R.S.2
  • 2
    • 0001780722 scopus 로고
    • Conversion of methanol and methylamines to methane and carbon dioxide
    • (Ferry, J.G., ed.), Chapman & Hall, Inc., New York
    • 2. 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, Inc., New York.
    • (1993) Methanogenesis , pp. 253-303
    • Keltjens, J.T.1    Vogels, G.D.2
  • 3
    • 0031024751 scopus 로고    scopus 로고
    • Methanol: Coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1
    • 3. 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
  • 4
    • 0030879503 scopus 로고    scopus 로고
    • Methanol: Coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol: Cob(I)alamin methyltransferase reaction
    • 4. Sauer, K. & Thauer, R.K. (1997) Methanol: coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol: cob(I)alamin methyltransferase reaction. Eur. J. Biochem. 249, 280-285.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 280-285
    • Sauer, K.1    Thauer, R.K.2
  • 5
    • 0024962345 scopus 로고
    • Different isozymes of methylcobalamin: 2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri
    • 5. Grahame, D.A. (1989) Different isozymes of methylcobalamin: 2-mercaptoethanesulfonate methyltransferase predominate in methanol-versus acetate-grown Methanosarcina barkeri. J. Biol. Chem. 264, 12890-12894.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12890-12894
    • Grahame, D.A.1
  • 6
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide: Coenzyme M methyltransferase isozymes from Methanosarcina barkeri
    • 6. LeClerc, G.M. & Grahame, D.A. (1996) Methylcobamide: coenzyme M methyltransferase isozymes from Methanosarcina barkeri. J. Biol. Chem. 271, 18725-18731.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 7
    • 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
    • 7. Harms, U. & Thauer, R.K. (1996) 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
  • 8
    • 0032079887 scopus 로고    scopus 로고
    • Methanol: Coenzyme M methyltransferase from Methanosarcina barkeri. Identification of the active-site histidine in the corrinoid-harboring subunit MtaC by site-directed mutagenesis
    • 8. Sauer, K. & Thauer, R.K. (1998) Methanol: coenzyme M methyltransferase from Methanosarcina barkeri. Identification of the active-site histidine in the corrinoid-harboring subunit MtaC by site-directed mutagenesis. Eur. J. Biochem. 253, 698-705.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 698-705
    • Sauer, K.1    Thauer, R.K.2
  • 10
    • 0027471227 scopus 로고
    • Involvement of an activation protein in the methanol: 2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri
    • 10. Daas, P.J.H., Gerrits, K.A.A., Keltjens, J.T., van der Drift, C. & Vogels, G.D. (1993) Involvement of an activation protein in the methanol: 2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri. J. Bacteriol. 175, 1278-1283.
    • (1993) J. Bacteriol. , vol.175 , pp. 1278-1283
    • Daas, P.J.H.1    Gerrits, K.A.A.2    Keltjens, J.T.3    Van Der Drift, C.4    Vogels, G.D.5
  • 11
    • 0027944948 scopus 로고
    • Characterization and determination of the redox properties of the 2[4Fe-4S] ferredoxin from Methanosarcina barkeri strain MS
    • 11. Daas, P.J.H., Hagen, W.R. & Vogels, G.D. (1994) Characterization and determination of the redox properties of the 2[4Fe-4S] ferredoxin from Methanosarcina barkeri strain MS. FEBS Lett. 356, 342-344.
    • (1994) FEBS Lett. , vol.356 , pp. 342-344
    • Daas, P.J.H.1    Hagen, W.R.2    Vogels, G.D.3
  • 12
    • 0029787826 scopus 로고    scopus 로고
    • Activation mechanism of methanol: 5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
    • 12. 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, 22346-22351.
    • (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
  • 13
    • 0029809057 scopus 로고    scopus 로고
    • Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol: 2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri
    • 13. Daas, P.J.H., Wassenaar, R.W., Willemsen, P., Theunissen, R.J., Keltjens. J.T., van der Drift, C. & Vogels, G.D. (1996) Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol: 2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri. J. Biol. Chem. 271, 22339-22345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22339-22345
    • Daas, P.J.H.1    Wassenaar, R.W.2    Willemsen, P.3    Theunissen, R.J.4    Keltjens, J.T.5    Van Der Drift, C.6    Vogels, G.D.7
  • 14
    • 0027157321 scopus 로고
    • Function of methylcobalamin: Coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri
    • 14. Yeliseev, A., Gärtner, P., Harms, U., Linder, D. & Thauer, R.K. (1993) Function of methylcobalamin: coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri. Arch. Microbiol. 159, 530-536.
    • (1993) Arch. Microbiol. , vol.159 , pp. 530-536
    • Yeliseev, A.1    Gärtner, P.2    Harms, U.3    Linder, D.4    Thauer, R.K.5
  • 15
    • 0030946069 scopus 로고    scopus 로고
    • Reconstitution of monomethylamine: Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri
    • 15. Burke, S.A. & Krzycki, J.A. (1997) Reconstitution of monomethylamine: coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 272, 16570-16577.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16570-16577
    • Burke, S.A.1    Krzycki, J.A.2
  • 16
    • 0031799184 scopus 로고    scopus 로고
    • Clustered genes encoding the melhyltransferase of methanogenesis from monomethylamine
    • 16. Burke, S.A., Lo, S.L. & Krzycki, J.A. (1998) Clustered genes encoding the melhyltransferase of methanogenesis from monomethylamine. J. Bacteriol. 180, 3432-3440.
    • (1998) J. Bacteriol. , vol.180 , pp. 3432-3440
    • Burke, S.A.1    Lo, S.L.2    Krzycki, J.A.3
  • 17
    • 0029864728 scopus 로고    scopus 로고
    • Specific roles of methylcobamide: Coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
    • 17. Ferguson, D.J. Jr, Krzycki, J.A. & Grahame, D.A. (1996) Specific roles of methylcobamide: coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri. J. Biol. Chem. 271, 5189-5194.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5189-5194
    • Ferguson D.J., Jr.1    Krzycki, J.A.2    Grahame, D.A.3
  • 18
    • 0029850006 scopus 로고    scopus 로고
    • Involvement of methyltransferase-activating protein and methyltransferase 2 isoenzyme II in methylamine: Coenzyme M methyltransferase reactions in Methanosarcina barkeri Fusaro
    • 18. Wassenaar, R.W., Daas, P.J.H., Geerts, W.J., Keltjens, J.T. & van der Drift, C. (1996) Involvement of methyltransferase-activating protein and methyltransferase 2 isoenzyme II in methylamine: coenzyme M methyltransferase reactions in Methanosarcina barkeri Fusaro. J. Bacteriol. 178, 6937-6944.
    • (1996) J. Bacteriol. , vol.178 , pp. 6937-6944
    • Wassenaar, R.W.1    Daas, P.J.H.2    Geerts, W.J.3    Keltjens, J.T.4    Van Der Drift, C.5
  • 19
    • 0032080258 scopus 로고    scopus 로고
    • Purification and characterization of dimethylamine: 5-hydroxybenzimidazlylcobamide methyltransferase from Methanosarcina barkeri Fusaro
    • 19. Wassenaar, R.W., Keltjens, J.T., van der Drift, C. & Vogels, G.D. (1998) Purification and characterization of dimethylamine: 5-hydroxybenzimidazlylcobamide methyltransferase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 253, 692-697.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 692-697
    • Wassenaar, R.W.1    Keltjens, J.T.2    Van Der Drift, C.3    Vogels, G.D.4
  • 20
    • 0031691338 scopus 로고    scopus 로고
    • Tetramethylammoium: Coenzyme M methyltransferase system from Methanococcoides sp
    • 20. Asakawa, S., Sauer, K., Liesack, W. & Thauer, R.K. (1998) Tetramethylammoium: coenzyme M methyltransferase system from Methanococcoides sp. Arch. Microbiol. 170, 220-226.
    • (1998) Arch. Microbiol. , vol.170 , pp. 220-226
    • Asakawa, S.1    Sauer, K.2    Liesack, W.3    Thauer, R.K.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 21. 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
  • 22
    • 0014429125 scopus 로고
    • A specific and sensitive assay for disulfides
    • 22. Zahler, W.L. & Cleland, W.W. (1968) A specific and sensitive assay for disulfides. J. Biol. Chem. 243, 716-719.
    • (1968) J. Biol. Chem. , vol.243 , pp. 716-719
    • Zahler, W.L.1    Cleland, W.W.2
  • 24
    • 0030829339 scopus 로고    scopus 로고
    • Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethioníne
    • 24. 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 adenosylmethioníne. Biochemistry 36, 8082-8091.
    • (1997) Biochemistry , vol.36 , pp. 8082-8091
    • Goulding, C.W.1    Postigo, D.2    Matthews, R.G.3
  • 25
    • 0001693812 scopus 로고
    • Reductive activation of the methyl-tetrahydromethanopterin: Coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH
    • 25. Kengen, S.W.M., Mosterd, J.J., Nelissen, R.L.H., Keltjens, J.T., van der Drift, C. & Vogels, G.D. (1988) Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH. Arch. Microbiol. 150, 405-412.
    • (1988) Arch. Microbiol. , vol.150 , pp. 405-412
    • Kengen, S.W.M.1    Mosterd, J.J.2    Nelissen, R.L.H.3    Keltjens, J.T.4    Van Der Drift, C.5    Vogels, G.D.6
  • 29
    • 0014373462 scopus 로고
    • The photolability of Co-alkylcobinamides
    • 29. Pailes, W.H. & Hogenkamp, H.P.C. (1968) The photolability of Co-alkylcobinamides. Biochemistry 7, 4160-4166.
    • (1968) Biochemistry , vol.7 , pp. 4160-4166
    • Pailes, W.H.1    Hogenkamp, H.P.C.2
  • 32
    • 0032554640 scopus 로고    scopus 로고
    • Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin
    • 32. Jarrett, J.T., Huang, S. & Matthews, R.G. (1998) Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin. Biochemistry 37, 5372-5382.
    • (1998) Biochemistry , vol.37 , pp. 5372-5382
    • Jarrett, J.T.1    Huang, S.2    Matthews, R.G.3
  • 33
    • 0025697224 scopus 로고
    • Participation of cob(I)alamin in the reaction catalyzed by methionine synthase from Escherichia coli: A steady-state and rapid reaction kinetic analysis
    • 33. Banerjee, R.V., Frasca, V., Ballou, D.P. & Matthews, R.G. (1990) Participation of cob(I)alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry 29, 11101-11109.
    • (1990) Biochemistry , vol.29 , pp. 11101-11109
    • Banerjee, R.V.1    Frasca, V.2    Ballou, D.P.3    Matthews, R.G.4
  • 34
    • 0002589303 scopus 로고    scopus 로고
    • 12 coenzymes, the central theme
    • (Kräutler, B., Arígoni, D. & Golding, B.T., eds.), Wiley-VCH, Weinheim, Germany
    • 12-Proteins (Kräutler, B., Arígoni, D. & Golding, B.T., eds.), pp. 3-44, Wiley-VCH, Weinheim, Germany.
    • (1998) 12-Proteins , pp. 3-44
    • Kräutler, B.1


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