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ENZYME

ENZYME entry: EC 1.14.19.3

Accepted Name
acyl-CoA 6-desaturase
Alternative Name(s)
Delta(6)-acyl CoA desaturase
Delta(6)-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
  • (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
  • (9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
Comment(s)
  • 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.
  • Formerly EC 1.14.99.25.
Cross-references
BRENDA1.14.19.3
EC2PDB1.14.19.3
ExplorEnz1.14.19.3
PRIAM enzyme-specific profiles1.14.19.3
KEGG Ligand Database for Enzyme Nomenclature1.14.19.3
IUBMB Enzyme Nomenclature1.14.19.3
IntEnz1.14.19.3
MEDLINEFind literature relating to 1.14.19.3
MetaCyc1.14.19.3
Rhea expert-curated reactions1.14.19.3
UniProtKB/Swiss-Prot
B2KKL4, FAD1_SIGCAA4FV48, FADS2_BOVINQ9DEX7, FADS2_DANRE
O95864, FADS2_HUMANQ4R749, FADS2_MACFAQ9Z0R9, FADS2_MOUSE
B8R1K0, FADS2_PAPANQ5REA7, FADS2_PONABQ9Z122, FADS2_RAT
A0A0C5PRW9, FADS2_TACFUQ23221, FAT3_CAEELQ08871, LLCD_SYNY3

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