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 | Glutaryl-CoA dehydrogenase, mitochondrial |
Enzyme Information
| 1.3.8.6 |
Glutaryl-CoA dehydrogenase (ETF).
based on mapping to UniProt Q92947
Glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO(2) + reduced electron-transfer flavoprotein.
-!- The enzyme catalyzes the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5). -!- FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. -!- The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyzes the oxidation to glutaconyl-CoA (EC 1.3.99.32). -!- Formerly EC 1.3.99.7.
|
UniProtKB Entries (1)
| Q92947 |
GCDH_HUMAN
Homo sapiens
Glutaryl-CoA dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 2R0N |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.
Biochemistry
|
