ENZYME entry: EC 1.3.8.8
| Accepted Name |
|---|
| long-chain-acyl-CoA dehydrogenase.
|
| Reaction catalysed |
|---|
| a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] <=> a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein] |
| Comment(s) |
|---|
- 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 6 to at least 16 carbon atoms.
- The highest activity was found with C12, and the rates with C8 and
C16 were 80% and 70%, respectively.
- The enzyme from rat can accept substrates with C8-C22.
- It is most active with C14 and C16, and has no activity with C4,
C6 or C24.
- cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
- Formerly EC 1.3.99.3 and EC 1.3.99.13.
|
| Cross-references |
|---|
| BRENDA | 1.3.8.8 |
| EC2PDB | 1.3.8.8 |
| ExplorEnz | 1.3.8.8 |
| PRIAM enzyme-specific profiles | 1.3.8.8 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.3.8.8 |
| IUBMB Enzyme Nomenclature | 1.3.8.8 |
| IntEnz | 1.3.8.8 |
| MEDLINE | Find literature relating to 1.3.8.8 |
| MetaCyc | 1.3.8.8 |
| Rhea expert-curated reactions | 1.3.8.8 |
| UniProtKB/Swiss-Prot |
| P28330, ACADL_HUMAN; | Q60HI0, ACADL_MACFA; | P51174, ACADL_MOUSE; |
| P79274, ACADL_PIG; | P15650, ACADL_RAT; | Q3L887, FADE5_MYCS2; |
| O53666, FADE5_MYCTU; | Q8X7R2, FADE_ECO57; | Q47146, FADE_ECOLI; |
| Q8Z937, FADE_SALTI; | Q8ZRJ7, FADE_SALTY; | Q8ZBY6, FADE_YERPE; |
|
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UniProtKB/Swiss-Prot entries corresponding to 1.3.8.-
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