| Entry |
|
| Name |
2-enoate reductase;
enoate reductase |
| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
butanoate:NAD+ Delta2-oxidoreductase |
| Reaction(IUBMB) |
butanoate + NAD+ = 2-butenoate + NADH + H+ [RN:R01689] |
| Reaction(KEGG) |
R01689;
(other) R02252
 |
| Substrate |
butanoate [CPD:C00246];
NAD+ [CPD:C00003] |
| Product |
2-butenoate [CPD:C01771];
NADH [CPD:C00004];
H+ [CPD:C00080] |
| Cofactor |
FAD [CPD:C00016];
Iron [CPD:C00023];
Sulfur [CPD:C00087];
Iron-sulfur [CPD:C00824] |
| Comment |
An iron-sulfur-flavoprotein (FAD). Acts (in the reverse direction)
on a wide range of alkyl and aryl alphabeta-unsaturated carboxylate
ions; 2-butenoate was the best substrate tested. |
| Pathway |
PATH: ec00360 Phenylalanine metabolism |
| Orthology |
KO: K10797 2-enoate reductase |
Reference Authors Title
Journal Organism
|
1 [PMID:477658]
Tischer W, Bader J, Simon H.
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 (1979) 103-12.
Clostridium kluyveri [GN:ckl], Clostridium sp. |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.3.1.31
IUBMB Enzyme Nomenclature: 1.3.1.31
ExPASy - ENZYME nomenclature database: 1.3.1.31
BRENDA, the Enzyme Database: 1.3.1.31
CAS: 70712-51-5 |