ENZYME entry: EC 1.3.8.7
Accepted Name |
medium-chain acyl-CoA dehydrogenase.
|
Alternative Name(s) |
acyl CoA dehydrogenase. |
acyl coenzyme A dehydrogenase. |
acyl dehydrogenase. |
fatty-acyl-CoA dehydrogenase. |
fatty acyl coenzyme A dehydrogenase. |
general acyl CoA dehydrogenase. |
Reaction catalysed |
a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] <=> a medium-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 4 to 16 carbon atoms, but is most active with C8 to C12
compounds.
- The enzyme from rat does not accept C16 at all and is most active
with C6-C8 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.
|
Cross-references |
BRENDA | 1.3.8.7 |
EC2PDB | 1.3.8.7 |
ExplorEnz | 1.3.8.7 |
PRIAM enzyme-specific profiles | 1.3.8.7 |
KEGG Ligand Database for Enzyme Nomenclature | 1.3.8.7 |
IUBMB Enzyme Nomenclature | 1.3.8.7 |
IntEnz | 1.3.8.7 |
MEDLINE | Find literature relating to 1.3.8.7 |
MetaCyc | 1.3.8.7 |
Rhea expert-curated reactions | 1.3.8.7 |
UniProtKB/Swiss-Prot |
A8XNF0, ACAD1_CAEBR; | A8WP91, ACAD2_CAEBR; | Q3SZB4, ACADM_BOVIN; |
Q22347, ACADM_CAEEL; | Q9VSA3, ACADM_DROME; | P11310, ACADM_HUMAN; |
Q8HXY8, ACADM_MACFA; | P45952, ACADM_MOUSE; | A5A6I0, ACADM_PANTR; |
P41367, ACADM_PIG; | P08503, ACADM_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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