2-enoate reductase
| 2-enoate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.31 | ||||||||
| CAS no. | 70712-51-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, 2-enoate reductase (EC 1.3.1.31) is an enzyme that catalyzes the chemical reaction of α,β-unsaturated carboxylic acids. Crotonic acid is a typical example:[1]
The three substrates of this enzyme are crotonic acid, reduced nicotinamide adenine dinucleotide (NADH), and a proton. Its products are butyric acid and oxidised NAD+.[2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanoate:NAD+ Delta2-oxidoreductase. This enzyme is also called enoate reductase. This enzyme participates in phenylalanine metabolism. It has cofactors: flavin adenine dinucleotide and iron–sulfur protein.[1]
References
- ^ a b Enzyme 1.3.1.31 at KEGG Pathway Database.
- ^ Tischer W, Bader J, Simon H (1979). "Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of alpha, beta-unsaturated carboxylate anions". Eur. J. Biochem. 97 (1): 103–12. doi:10.1111/j.1432-1033.1979.tb13090.x. PMID 477658.