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Information on EC 1.14.19.12 - acyl-lipid omega-(9-4) desaturase

for references in articles please use BRENDA:EC1.14.19.12
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IUBMB Comments
The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in omega9 unsaturated C18 or C20 fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing omega9 bond, towards the carboxy end of the fatty acid (at the omega13 position). When acting on 20:2Delta(11,14) and 20:3Delta(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.
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The expected taxonomic range for this enzyme is: Chlamydomonas reinhardtii
Synonyms
omega13 desaturase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = coniferonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
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(2)
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linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = pinolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
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(1)
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PATHWAY SOURCE
PATHWAYS
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