EC 1.14.19.12 - Acyl-lipid ω-(9−4) desaturase

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IntEnz Enzyme Nomenclature
EC 1.14.19.12

Names

Accepted name:
acyl-lipid ω-(9−4) desaturase
Other names:
acyl-lipid ω-13 desaturase
acyl-lipid 7-desaturase [ambiguous]
Systematic name:
acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase [ω(9−4),ω(9−5) cis-dehydrogenating]

Reactions

Comments:

The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in ω9 unsaturated C18 or C20 fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing ω9 bond, towards the carboxy end of the fatty acid (at the ω13 position). When acting on 20:2Δ(11,14) and 20:3Δ(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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Kajikawa, M., Yamato, K. T., Kohzu, Y., Shoji, S., Matsui, K., Tanaka, Y., Sakai, Y., Fukuzawa, H.
    A front-end desaturase from Chlamydomonas reinhardtii produces pinolenic and coniferonic acids by omega13 desaturation in methylotrophic yeast and tobacco.
    Plant Cell Physiol. 47 : 64-73 (2006). [PMID: 16267098]

[EC 1.14.19.12 created 2015]