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ENZYME entry: EC 1.14.19.12

Accepted Name
Acyl-lipid omega-(9-4) desaturase.
Alternative Name(s)
Acyl-lipid 7-desaturase.
Acyl-lipid omega-13 desaturase.
Reaction catalysed
  • Linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> pinolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
  • Alpha-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> coniferonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
Comment(s)
  • The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in omega(9) unsaturated C(18) or C(20) fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing omega(9) bond, toward the carboxy end of the fatty acid (at the omega(13) position).
  • When acting on 20:2-Delta-(11,14) and 20:3-Delta-(11,14,17) substrates it introduces the new double bond between carbons 7 and 8.
  • The enzyme contains a cytochrome b5 domain that acts as the direct electron donor for the active site of the desaturase.
Cross-references
BRENDA1.14.19.12
EC2PDB1.14.19.12
ExplorEnz1.14.19.12
PRIAM enzyme-specific profiles1.14.19.12
KEGG Ligand Database for Enzyme Nomenclature1.14.19.12
IUBMB Enzyme Nomenclature1.14.19.12
IntEnz1.14.19.12
MEDLINEFind literature relating to 1.14.19.12
MetaCyc1.14.19.12
UniProtKB/Swiss-Prot
Q2HWK7, DES_CHLRE

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