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ENZYME

ENZYME entry: EC 1.3.8.8

PURL: https://purl.expasy.org/enzyme/EC/1.3.8.8
Accepted Name
long-chain-acyl-CoA dehydrogenase
Reaction catalysed
a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 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
BRENDA1.3.8.8
EC2PDB1.3.8.8
ExplorEnz1.3.8.8
KEGG Ligand Database for Enzyme Nomenclature1.3.8.8
IUBMB Enzyme Nomenclature1.3.8.8
MEDLINEFind literature relating to 1.3.8.8
MetaCyc1.3.8.8
Rhea expert-curated reactions1.3.8.8
UniProtKB/Swiss-Prot
Q9H845, ACAD9_HUMANQ8JZN5, ACAD9_MOUSEB1WC61, ACAD9_RAT
P28330, ACADL_HUMANQ60HI0, ACADL_MACFAP51174, ACADL_MOUSE
P79274, ACADL_PIGP15650, ACADL_RATP48818, ACADV_BOVIN
P49748, ACADV_HUMANQ8HXY7, ACADV_MACFAP50544, ACADV_MOUSE
P45953, ACADV_RATQ5ZHT1, ACD11_CHICKQ709F0, ACD11_HUMAN
Q80XL6, ACD11_MOUSEQ5R778, ACD11_PONABB3DMA2, ACD11_RAT
A0AAD6J5T3, ACD_DREDAQ3L887, FADE5_MYCS2O53666, FADE5_MYCTU
Q8X7R2, FADE_ECO57Q47146, FADE_ECOLIQ8Z937, FADE_SALTI
Q8ZRJ7, FADE_SALTYQ8ZBY6, FADE_YERPE

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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.-.-.-