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 | very long-chain specific acyl-CoA dehydrogenase, mitochondrial |
Enzyme Information
| 1.3.8.9 |
Very-long-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P49748
A very-long-chain acyl-CoA + electron-transfer flavoprotein = a very- long-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 is most active toward long-chain acyl-CoAs such as C(14), C(16) and C(18), but is also active with very-long-chain acyl-CoAs up to 24 carbons. -!- It shows no activity for substrates of less than 12 carbons. -!- It's specific activity toward palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase. -!- cf. EC 1.3.8.1, EC 1.3.8.7 and EC 1.3.8.8. -!- Formerly EC 1.3.99.3.
|
UniProtKB Entries (1)
| P49748 |
ACADV_HUMAN
Homo sapiens
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 3B96 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.
J.Biol.Chem.
|
