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ENZYME entry: EC 1.14.19.4

Accepted Name
Acyl-lipid (11-3)-desaturase.
Alternative Name(s)
Acyl-lipid 8-desaturase.
Delta(8)-desaturase.
SLD.
Reaction catalysed
  • An (11Z,14Z)-icosa-11,14-dienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
  • An (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
Comment(s)
  • The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina, introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta(11) desaturation.
  • The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid.
  • It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
  • Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
Cross-references
PROSITEPDOC00170
BRENDA1.14.19.4
EC2PDB1.14.19.4
ExplorEnz1.14.19.4
PRIAM enzyme-specific profiles1.14.19.4
KEGG Ligand Database for Enzyme Nomenclature1.14.19.4
IUBMB Enzyme Nomenclature1.14.19.4
IntEnz1.14.19.4
MEDLINEFind literature relating to 1.14.19.4
MetaCyc1.14.19.4
Rhea expert-curated reactions1.14.19.4
UniProtKB/Swiss-Prot
Q9SWQ9, SLD1_EUGGR

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