ENZYME entry: EC 1.3.8.8
Accepted Name |
Long-chain-acyl-CoA dehydrogenase.
|
Reaction catalysed |
Long-chain-acyl-CoA + electron-transfer flavoprotein <=> long-chain-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Cofactor(s) |
FAD.
|
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 C(12), and the rates with C(8)
and C(16) were 80% and 70%, respectively.
- The enzyme from rat can accept substrates with C(8)-C(22).
- It is most active with C(14) and C(16), and has no activity with
C(4), C(6) or C(24).
- 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 |
PROSITE | PDOC00070 |
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; |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.3.8.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-