Coenzyme-B sulfoethylthiotransferase

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In enzymology, a coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1) is an enzyme that catalyzes the chemical reaction

2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) $\rightleftharpoons$ CoM-S-S-CoB + methane

Thus, the two substrates of this enzyme are 2-(methylthio)ethanesulfonate and N-(7-mercaptoheptanoyl)threonine 3-O-phosphate, whereas its two products are CoM-S-S-CoB and 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.

[edit] References

IUBMB entry for 2.8.4.1
BRENDA references for 2.8.4.1 (Recommended.)
PubMed references for 2.8.4.1
PubMed Central references for 2.8.4.1
Google Scholar references for 2.8.4.1
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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: 63–68.
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: 1457–62. doi:10.1126/science.278.5342.1457. 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: 3508–16. doi:10.1002/1521-3765(20001002)6:19<3508::AID-CHEM3508>3.0.CO;2-W. PMID 11072815.