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EC 1.14.19.12 Details
show Brenda entryEC number
1.14.19.12
Accepted name
acyl-lipid ω-(9-4) desaturase
Reaction
(1) linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = pinolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O;;(2) α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = coniferonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O;;
Other name(s)
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]
Comment
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.
History
created 2015
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.14.1.2 created 1965, deleted 1972 1.14.1.4 created 1965, deleted 1972 1.14.1.5 created 1965, deleted 1972 1.14.1.7 created 1965, deleted 1972 1.14.1.8 created 1965, deleted 1972 1.14.1.9 created 1965, deleted 1972 1.14.1.10 created 1965, deleted 1972 1.14.1.11 created 1965, deleted 1972
