2-(R)-hydroxypropyl-CoM dehydrogenase
| 2-(R)-hydroxypropyl-CoM dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.268 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 2-(R)-hydroxypropyl-CoM dehydrogenase (EC 1.1.1.268) is an enzyme that catalyzes the chemical reaction
- 2-(R)-hydroxypropyl-CoM + NAD+ 2-oxopropyl-CoM + NADH + H+
Thus, the two substrates of this enzyme are 2-(R)-hydroxypropyl-CoM and NAD+, whereas its 3 products are 2-oxopropyl-CoM, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase. This enzyme is also called 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CFC.
References
[edit]- 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.
