EC - Acyl-lipid (11-3)-desaturase

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IntEnz Enzyme Nomenclature


Accepted name:
acyl-lipid (11-3)-desaturase
Other names:
efd1 (gene name)
Δ8 fatty acid desaturase
acyl-lipid 8-desaturase
Δ8-fatty-acid desaturase
D8Des (gene name)
phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase [incorrect]
Systematic name:
acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase [(11-3),(11-2) cis-dehydrogenating]



The enzyme, characterized from the protist Euglena gracilis [1] and the microalga Rebecca salina [2], introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Δ11 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00170
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102003


  1. Wallis, J.G. and Browse, J.
    The Δ8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids.
    Arch. Biochem. Biophys. 365 : 307-316 (1999). [PMID: 10328826]
  2. Zhou, X. R., Robert, S. S., Petrie, J. R., Frampton, D. M., Mansour, M. P., Blackburn, S. I., Nichols, P. D., Green, A. G., Singh, S. P.
    Isolation and characterization of genes from the marine microalga Pavlova salina encoding three front-end desaturases involved in docosahexaenoic acid biosynthesis.
    Phytochemistry 68 : 785-796 (2007). [PMID: 17291553]

[EC created 2008, modified 2015]