ENZYME entry: EC 1.14.19.4
Accepted Name |
Acyl-lipid (11-3)-desaturase.
|
Alternative Name(s) |
Acyl-lipid 8-desaturase. |
Delta(8)-desaturase. |
SLD. |
Reaction catalysed |
- An (11Z,14Z)-icosa-11,14-dienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
- An (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H(2)O
|
Comment(s) |
- The enzyme, characterized from the protist Euglena gracilis and the
microalga Rebecca salina, introduces a cis double bond at the
8-position in 20-carbon fatty acids that are incorporated into a
glycerolipid and have an existing Delta(11) desaturation.
- The enzyme is a front-end desaturase, introducing the new double bond
between the pre-existing double bond and the carboxyl-end of the
fatty acid.
- It contains a cytochrome b5 domain that acts as the direct electron
donor to the active site of the desaturase, and does not require an
external cytochrome.
- Involved in alternative pathways for the biosynthesis of the
polyunsaturated fatty acids arachidonate and icosapentaenoate.
|
Cross-references |
PROSITE | PDOC00170 |
BRENDA | 1.14.19.4 |
EC2PDB | 1.14.19.4 |
ExplorEnz | 1.14.19.4 |
PRIAM enzyme-specific profiles | 1.14.19.4 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.19.4 |
IUBMB Enzyme Nomenclature | 1.14.19.4 |
IntEnz | 1.14.19.4 |
MEDLINE | Find literature relating to 1.14.19.4 |
MetaCyc | 1.14.19.4 |
Rhea expert-curated reactions | 1.14.19.4 |
UniProtKB/Swiss-Prot |
|
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