ID   1.3.8.8
DE   long-chain-acyl-CoA dehydrogenase.
CA   a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer
CA   flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-
CA   transfer flavoprotein].
CC   -!- One of several enzymes that catalyze the first step in fatty acids
CC       beta-oxidation.
CC   -!- The enzyme from pig liver can accept substrates with acyl chain
CC       lengths of 6 to at least 16 carbon atoms.
CC   -!- The highest activity was found with C12, and the rates with C8 and
CC       C16 were 80% and 70%, respectively.
CC   -!- The enzyme from rat can accept substrates with C8-C22.
CC   -!- It is most active with C14 and C16, and has no activity with C4,
CC       C6 or C24. cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
CC   -!- Formerly EC 1.3.99.3 and EC 1.3.99.13.
DR   Q9H845, ACAD9_HUMAN;  Q8JZN5, ACAD9_MOUSE;  B1WC61, ACAD9_RAT  ;
DR   P28330, ACADL_HUMAN;  Q60HI0, ACADL_MACFA;  P51174, ACADL_MOUSE;
DR   P79274, ACADL_PIG  ;  P15650, ACADL_RAT  ;  P48818, ACADV_BOVIN;
DR   P49748, ACADV_HUMAN;  Q8HXY7, ACADV_MACFA;  P50544, ACADV_MOUSE;
DR   P45953, ACADV_RAT  ;  Q5ZHT1, ACD11_CHICK;  Q709F0, ACD11_HUMAN;
DR   Q80XL6, ACD11_MOUSE;  Q5R778, ACD11_PONAB;  B3DMA2, ACD11_RAT  ;
DR   A0AAD6J5T3, ACD_DREDA  ;  Q3L887, FADE5_MYCS2;  O53666, FADE5_MYCTU;
DR   Q8X7R2, FADE_ECO57 ;  Q47146, FADE_ECOLI ;  Q8Z937, FADE_SALTI ;
DR   Q8ZRJ7, FADE_SALTY ;  Q8ZBY6, FADE_YERPE ;
//