2-oxopropyl-CoM reductase (carboxylating)
| 2-oxopropyl-CoM reductase (carboxylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.1.5 | ||||||||
| 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 | ||||||||
| |||||||||
2-oxopropyl-CoM reductase (carboxylating) (EC 1.8.1.5) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are 2-mercaptoethanesulfonic acid (Coenzyme M), acetoacetic acid, and nicotinamide adenine dinucleotide phosphate (NADP+). Its products are 2-acetylthioethanesulfonic acid (2-oxopropyl-Coenzyme M), carbon dioxide, reduced NADPH, and a proton.[1][2][3]
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
- ^ Enzyme 1.8.1.5 at KEGG Pathway Database.
- ^ 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 [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system". Biochemistry. 39 (6): 1294–304. doi:10.1021/bi992282p. PMID 10684609.