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ENZYME entry: EC

Accepted Name
Acyl-CoA 6-desaturase.
Alternative Name(s)
Delta(6)-acyl CoA desaturase.
Delta(6)-fatty acyl-CoA desaturase.
Fatty acid 6-desaturase.
Fatty acid Delta(6)-desaturase.
Linoleate desaturase.
Linoleic acid desaturase.
Linoleoyl CoA desaturase.
Linoleoyl-CoA desaturase.
Linoleoyl-coenzyme A desaturase.
Long-chain fatty acid Delta(6)-desaturase.
Reaction catalysed
  • Linoleoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O
  • Alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O
Fe cation.
  • The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs.
  • It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid.
  • The human enzyme has a broad substrate range; it also acts on palmitoyl-CoA, generating sapienoyl-CoA, and on (9Z,12Z,15Z,18Z,21Z)- tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate.
  • The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
PRIAM enzyme-specific profiles1.14.19.3
KEGG Ligand Database for Enzyme Nomenclature1.14.19.3
IUBMB Enzyme Nomenclature1.14.19.3
MEDLINEFind literature relating to
Rhea expert-curated reactions1.14.19.3
O95864, FADS2_HUMAN;  Q4R749, FADS2_MACFA;  Q9Z0R9, FADS2_MOUSE;  
A0A0C5PRW9, FADS2_TACFU;  Q23221, FAT3_CAEEL;  Q08871, LLCD_SYNY3;  

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