2-oxopropyl-CoM reductase (carboxylating)

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In enzymology, a 2-oxopropyl-CoM reductase (carboxylating) (EC 1.8.1.5) is an enzyme that catalyzes the chemical reaction

2-mercaptoethanesulfonate + acetoacetate + NADP⁺ $\rightleftharpoons$ 2-(2-oxopropylthio)ethanesulfonate + CO₂ + NADPH

The 3 substrates of this enzyme are 2-mercaptoethanesulfonate, acetoacetate, and NADP⁺, whereas its 3 products are 2-(2-oxopropylthio)ethanesulfonate, CO₂, and NADPH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-mercaptoethanesulfonate,acetoacetate:NADP+ oxidoreductase (decarboxylating). Other names in common use include NADPH:2-(2-ketopropylthio)ethanesulfonate, oxidoreductase/carboxylase, and NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2C3C and 2C3D.

[edit] References

IUBMB entry for 1.8.1.5
BRENDA references for 1.8.1.5 (Recommended.)
PubMed references for 1.8.1.5
PubMed Central references for 1.8.1.5
Google Scholar references for 1.8.1.5
Allen JR, Clark DD, Krum JG, Ensign SA (1999). "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation". Proc. Natl. Acad. Sci. U. S. A. 96: 8432–7. doi:10.1073/pnas.96.15.8432. PMID 10411892.
Clark DD, Allen JR, Ensign SA (2000). "Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system". Biochemistry. 39: 1294–304. doi:10.1021/bi992282p. PMID 10684609.