EC 2.8.4.1 - Coenzyme-B sulfoethylthiotransferase

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IntEnz Enzyme Nomenclature
EC 2.8.4.1

Names

Accepted name:
coenzyme-B sulfoethylthiotransferase
Other names:
methyl coenzyme M reductase
methyl-CoM reductase
Systematic name:
methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase

Reaction

Cofactor

Comments:

This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane. The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050524
UniProtKB/Swiss-Prot: (36) [show] [UniProt]

References

  1. Bobik, T.A., Olson, K.D., Noll, K.M. and Wolfe, R.S.
    Evidence that the heterodisulfide of coenzyme-M and 7-mercaptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium.
    Biochem. Biophys. Res. Commun. 149: 455-460 (1987). [PMID: 3122735]
  2. Ellermann, J., Hedderich, R., Böcher, R. and Thauer, R.K.
    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 (1988). [PMID: 3350018]
  3. Ermler, U., Grabarse, W., Shima, S., Goubeaud, M. and Thauer, R.K.
    Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation.
    Science 278: 1457-1462 (1997). [PMID: 9367957]
  4. Signor, L., Knuppe, C., Hug, R., Schweizer, B., Pfaltz, A. and Jaun, B.
    Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate - a process mimicking methanogenesis in Archaea.
    Chem. Eur. J. 6: 3508-3516 (2000). [PMID: 11072815]
  5. Scheller, S., Goenrich, M., Mayr, S., Thauer, R. K., Jaun, B.
    Intermediates in the catalytic cycle of methyl coenzyme M reductase: isotope exchange is consistent with formation of a σ-alkane-nickel complex.
    Angew. Chem. Int. Ed. Engl. 49: 8112-8115 (2010). [PMID: 20857468]

[EC 2.8.4.1 created 2001, modified 2011]