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ENZYME

ENZYME entry: EC 1.14.19.44

Accepted Name
acyl-CoA (8-3)-desaturase
Alternative Name(s)
acyl-CoA 5-desaturase (methylene-interrupted)
Reaction catalysed
  • (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
  • (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
Comment(s)
  • The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8.
  • The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyze the desaturation of dihomo-gamma-linoleate ((8Z,11Z,14Z)-icosa-8,11,14-trienoate) and (8Z,11Z,14Z,17Z)-icosa- 8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively.
  • The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37.
Cross-references
BRENDA1.14.19.44
EC2PDB1.14.19.44
ExplorEnz1.14.19.44
PRIAM enzyme-specific profiles1.14.19.44
KEGG Ligand Database for Enzyme Nomenclature1.14.19.44
IUBMB Enzyme Nomenclature1.14.19.44
IntEnz1.14.19.44
MEDLINEFind literature relating to 1.14.19.44
MetaCyc1.14.19.44
Rhea expert-curated reactions1.14.19.44
UniProtKB/Swiss-Prot
B2KKL4, FAD1_SIGCAD8X2C5, FAD2_SIGCAO60427, FADS1_HUMAN
Q920L1, FADS1_MOUSEA4UVI1, FADS1_PAPANQ920R3, FADS1_RAT
Q9DEX7, FADS2_DANREG5EG11, FAT4_CAEEL

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