| Entry |
|
|---|
| Name |
2-methyl-branched-chain-enoyl-CoA reductase |
|---|
| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
 |
|---|
| Sysname |
2-methyl-branched-chain-acyl-CoA:NAD+ 2-oxidoreductase |
|---|
| Reaction(IUBMB) |
2-methylbutanoyl-CoA + NAD+ = 2-methylcrotonoyl-CoA + NADH + H+
[RN:R03169] |
|---|
| Reaction(KEGG) |
R03169
 |
|---|
| Substrate |
2-methylbutanoyl-CoA [CPD:C01033];
NAD+ [CPD:C00003] |
|---|
| Product |
2-methylcrotonoyl-CoA;
NADH [CPD:C00004];
H+ [CPD:C00080] |
|---|
| Cofactor |
FAD [CPD:C00016] |
|---|
| Comment |
A flavoprotein (FAD) from Ascaris suum. The reaction proceeds only
in the presence of another flavoprotein ('electron-transferring
flavoprotein'). |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3988734]
Komuniecki R, Fekete S, Thissen-Parra J.
Purification and characterization of the 2-methyl branched-chain
Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent
enoyl-CoA reduction in anaerobic mitochondria of the nematode,
Ascaris suum.
J. Biol. Chem. 260 (1985) 4770-7.
Ascaris suum |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:2736251]
Komuniecki R, McCrury J, Thissen J, Rubin N.
Electron-transfer flavoprotein from anaerobic Ascaris suum
mitochondria and its role in NADH-dependent 2-methyl branched-chain
enoyl-CoA reduction.
Biochim. Biophys. Acta. 975 (1989) 127-31.
Ascaris suum |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.3.1.52
IUBMB Enzyme Nomenclature: 1.3.1.52
ExPASy - ENZYME nomenclature database: 1.3.1.52
BRENDA, the Enzyme Database: 1.3.1.52
CAS: 122320-06-3 |
|---|
