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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 ${\displaystyle \rightleftharpoons }$ 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.

Structural studies

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

References

• 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 (15): 8432–7. Bibcode:1999PNAS...96.8432A. doi:10.1073/pnas.96.15.8432. PMC 17533. PMID 10411892.
• Clark DD, Allen JR, Ensign SA (2000). "Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system". Biochemistry. 39 (6): 1294–304. doi:10.1021/bi992282p. PMID 10684609.

• Biology

• EC 1.8.1
• NADPH-dependent enzymes
• Enzymes of known structure