- 2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) CoM-S-S-CoB + methane
This enzyme belongs to the family of transferases, specifically those transferring alkylthio groups. The systematic name of this enzyme class is 2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreoni ne S-(2-sulfoethyl)thiotransferase. Other names in common use include methyl-CoM reductase, and methyl coenzyme M reductase. This enzyme participates in folate biosynthesis.
- IUBMB entry for 18.104.22.168
- BRENDA references for 22.214.171.124 (Recommended.)
- PubMed references for 126.96.36.199
- PubMed Central references for 188.8.131.52
- Google Scholar references for 184.108.40.206
- Bobik TA, Olson KD, Noll KM, Wolfe RS (1987). "Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium". Biochem. Biophys. Res. Commun. 149: 455&ndash, 60. PMID 3122735.
- Ellermann J, Hedderich R, Boecher R and Thauer RK (1988). "The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg)". Eur. J. Biochem. 184: 63&ndash, 68.
- Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK (1997). "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation". Science. 278: 1457&ndash, 62. PMID 9367957.
- Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B (2000). "Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate--a process mimicking methanogenesis in archaea". Chemistry. 6: 3508&ndash, 16. PMID 11072815.
Gene Ontology (GO) codes
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