CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.140 | Butyryl-CoA Dehydrogenase, subunit A; domain 3 |
|
1.20.140.10 | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
| Functional Family | Acyl-CoA dehydrogenase FadE25 |
Enzyme Information
| 1.3.8.1 |
Short-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P15651
A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
-!- One of several enzymes that catalyze the first step in fatty acids beta-oxidation. -!- The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R hydrogen atoms. -!- The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. -!- The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. -!- The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. -!- Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9. -!- Formerly EC 1.3.2.1 and EC 1.3.99.2.
|
UniProtKB Entries (1)
| P15651 |
ACADS_RAT
Rattus norvegicus
Short-chain specific acyl-CoA dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 1JQI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.
J.Biol.Chem.
|
