ENZYME entry: EC 1.14.19.12
Accepted Name |
Acyl-lipid omega-(9-4) desaturase.
|
Alternative Name(s) |
Acyl-lipid 7-desaturase. |
Acyl-lipid omega-13 desaturase. |
Reaction catalysed |
- Linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> pinolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
- Alpha-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> coniferonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
|
Comment(s) |
- The enzyme, characterized from the green alga Chlamydomonas
reinhardtii, is a front-end desaturase that introduces a cis double
bond in omega(9) unsaturated C(18) or C(20) fatty acids incorporated
into lipids, at a position 4 carbon atoms from the existing omega(9)
bond, toward the carboxy end of the fatty acid (at the omega(13)
position).
- When acting on 20:2-Delta-(11,14) and 20:3-Delta-(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.
|
Cross-references |
BRENDA | 1.14.19.12 |
EC2PDB | 1.14.19.12 |
ExplorEnz | 1.14.19.12 |
PRIAM enzyme-specific profiles | 1.14.19.12 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.19.12 |
IUBMB Enzyme Nomenclature | 1.14.19.12 |
IntEnz | 1.14.19.12 |
MEDLINE | Find literature relating to 1.14.19.12 |
MetaCyc | 1.14.19.12 |
Rhea expert-curated reactions | 1.14.19.12 |
UniProtKB/Swiss-Prot |
|
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