(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase
(Methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 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 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 methyl-CoM + [Co(I) methylamine-specific corrinoid protein]
This enzyme contains zinc.
References
- ↑ Burke, S.A.; Krzycki, J.A. (1995). "Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine". J. Bacteriol. 177: 4410–4416. PMID 7635826.
- ↑ 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: 18725–18731. doi:10.1074/jbc.271.31.18725. PMID 8702528.
- ↑ 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. PMID 9006042.
- ↑ Burke, S.A.; Lo, S.L.; Krzycki, J.A. (1998). "Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine". J. Bacteriol. 180: 3432–3440. PMID 9642198.
- ↑ Ferguson, D.J. Jr.; Gorlatova, N.; Grahame, D.A.; Krzycki, J.A. (2000). "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri". J. Biol. Chem. 275: 29053–29060. doi:10.1074/jbc.m910218199. PMID 10852929.
External links
- (methyl-Co(III) methylamine-specific corrinoid protein):coenzyme M methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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