A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

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 coenzyme A dehydrogenase.
Fatty-acyl-CoA dehydrogenase.
General acyl CoA dehydrogenase.
Reaction catalysed
A medium-chain acyl-CoA + electron-transfer flavoprotein <=> a medium-chain trans-2,3-dehydroacyl-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 C(8) to C(12) compounds.
  • The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) 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
BRENDA1.3.8.7
EC2PDB1.3.8.7
ExplorEnz1.3.8.7
PRIAM enzyme-specific profiles1.3.8.7
KEGG Ligand Database for Enzyme Nomenclature1.3.8.7
IUBMB Enzyme Nomenclature1.3.8.7
IntEnz1.3.8.7
MEDLINEFind literature relating to 1.3.8.7
MetaCyc1.3.8.7
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;  Q8X7R2, FADE_ECO57;  
Q47146, FADE_ECOLI;  Q8Z937, FADE_SALTI;  Q8ZRJ7, FADE_SALTY;  
Q8ZBY6, FADE_YERPE;  

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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.-.-.-