CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.110 | Butyryl-CoA Dehydrogenase, subunit A; domain 2 |
|
2.40.110.10 | Butyryl-CoA Dehydrogenase, subunit A, domain 2 |
Domain Context
CATH Clusters
| Superfamily | Butyryl-CoA Dehydrogenase, subunit A, domain 2 |
| Functional Family | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial |
Enzyme Information
| 1.3.8.7 |
Medium-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P11310
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-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 from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds. -!- The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds. -!- cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9. -!- Formerly EC 1.3.2.2 and EC 1.3.99.3.
|
UniProtKB Entries (1)
| P11310 |
ACADM_HUMAN
Homo sapiens
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 1EGE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Biochemistry
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