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ENZYME entry: EC 1.14.19.36

Accepted Name
sn-1 acyl-lipid omega-3 desaturase (ferredoxin).
Reaction catalysed
  • a 1-[(6Z,9Z,12Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] <=> a 1-[(6Z,9Z,12Z,15Z)-octadectetraenoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
  • a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] <=> a 1-[(9Z,12Z,15Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Comment(s)
  • The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 15 of linoleoyl and gamma-linolenoyl groups attached to the sn-1 position of glycerolipids.
  • The enzyme is an omega desaturase, and determines the location of the double bond by counting three carbons from the methyl end of the fatty acid.
  • It is non-specific with respect to the polar head group of the glycerolipid.
  • Cf. EC 1.14.19.35.
Cross-references
BRENDA1.14.19.36
EC2PDB1.14.19.36
ExplorEnz1.14.19.36
PRIAM enzyme-specific profiles1.14.19.36
KEGG Ligand Database for Enzyme Nomenclature1.14.19.36
IUBMB Enzyme Nomenclature1.14.19.36
IntEnz1.14.19.36
MEDLINEFind literature relating to 1.14.19.36
MetaCyc1.14.19.36
Rhea expert-curated reactions1.14.19.36

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.19.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-