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
PROSITEPDOC00070
BRENDA1.3.8.8
EC2PDB1.3.8.8
ExplorEnz1.3.8.8
PRIAM enzyme-specific profiles1.3.8.8
KEGG Ligand Database for Enzyme Nomenclature1.3.8.8
IUBMB Enzyme Nomenclature1.3.8.8
IntEnz1.3.8.8
MEDLINEFind literature relating to 1.3.8.8
MetaCyc1.3.8.8
UniProtKB/Swiss-Prot
P28330, ACADL_HUMAN;  Q60HI0, ACADL_MACFA;  P51174, ACADL_MOUSE;  
P79274, ACADL_PIG;  P15650, ACADL_RAT;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
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.-.-.-