(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase (EC 2.1.1.247, methyltransferase 2, MT2, MT2-A, mtbA (gene)) is an enzyme with systematic name methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.247 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M ⇌ methyl-CoM + [Co(I) methylamine-specific corrinoid protein]
This enzyme contains zinc.
References
edit- ^ Burke SA, Krzycki JA (August 1995). "Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine". Journal of Bacteriology. 177 (15): 4410–6. PMC 177191. PMID 7635826.
- ^ LeClerc GM, Grahame DA (August 1996). "Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression". The Journal of Biological Chemistry. 271 (31): 18725–31. doi:10.1074/jbc.271.31.18725. PMID 8702528.
- ^ Ferguson DJ, Krzycki JA (February 1997). "Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri". Journal of Bacteriology. 179 (3): 846–52. doi:10.1128/jb.179.3.846-852.1997. PMC 178769. PMID 9006042.
- ^ Burke SA, Lo SL, Krzycki JA (July 1998). "Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine". Journal of Bacteriology. 180 (13): 3432–40. PMC 107300. PMID 9642198.
- ^ Ferguson DJ, Gorlatova N, Grahame DA, Krzycki JA (September 2000). "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri". The Journal of Biological Chemistry. 275 (37): 29053–60. doi:10.1074/jbc.m910218199. PMID 10852929.
External links
edit- (methyl-Co(III)+methylamine-specific+corrinoid+protein):coenzyme+M+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)