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 | Acyl-CoA dehydrogenase, mitochondrial |
Enzyme Information
1.3.8.1 |
Short-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P16219
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.
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UniProtKB Entries (1)
P16219 |
ACADS_HUMAN
Homo sapiens
Short-chain specific acyl-CoA dehydrogenase, mitochondrial
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PDB Structure
PDB | 2VIG |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal Structure of Human Short-Chain Acyl Coa Dehydrogenase
To be Published
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