2-oxo-acid reductase
| 2-oxo-acid reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.99.30 | ||||||||
| CAS no. | 115299-99-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 2-oxo-acid reductase (EC 1.1.99.30) is an enzyme that catalyzes the chemical reaction
- a (2R)-hydroxy-carboxylate + acceptor a 2-oxo-carboxylate + reduced acceptor
Thus, the two substrates of this enzyme are (2R)-hydroxy-carboxylate and acceptor, whereas its two products are 2-oxo-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (2R)-hydroxy-carboxylate:acceptor oxidoreductase. Other names in common use include (2R)-hydroxycarboxylate-viologen-oxidoreductase, HVOR, and 2-oxoacid reductase.
References
[edit]- Trautwein T, Krauss F, Lottspeich F, Simon H (1994). "The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein". Eur. J. Biochem. 222 (3): 1025–32. doi:10.1111/j.1432-1033.1994.tb18954.x. PMID 8026480.
- Neumann S, Simon H (1985). "On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species". FEBS Lett. 167 (1): 29–32. doi:10.1016/0014-5793(84)80826-1.
