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1.14.19.12: acyl-lipid omega-(9-4) desaturase

This is an abbreviated version!
For detailed information about acyl-lipid omega-(9-4) desaturase, go to the full flat file.

Reaction

alpha-linolenoyl-[glycerolipid]
+ 2 ferrocytochrome b5 +
O2
+ 2 H+ =
coniferonoyl-[glycerolipid]
+ 2 ferricytochrome b5 + 2 H2O

Synonyms

acyl-lipid 7-desaturase, acyl-lipid omega-13 desaturase, DES, omega13 desaturase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
                1.14.19.12 acyl-lipid omega-(9-4) desaturase

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Resultsin table
1AA Sequence
1Cloned(Commentary)
1Cofactor
11Natural Substrates/ Products (Substrates)
2Organism
1Pathway
2Reaction
2Reference
11Substrates and Products (Substrate)
6Synonyms
1Systematic Name

Systematic Name

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

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SYSTEMATIC NAME
IUBMB Comments
acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase [omega(9-4),omega(9-5) cis-dehydrogenating]
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.