| Accepted Name |
|---|
| sn-1 acyl-lipid omega-3 desaturase (ferredoxin)
|
| Reaction catalysed |
|---|
- a 1-[(6Z,9Z,12Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] <=> a 1-[(6Z,9Z,12Z,15Z)-octadectetraenoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
- a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] <=> a 1-[(9Z,12Z,15Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
|
| Comment(s) |
|---|
- The enzyme, characterized from cyanobacteria, introduces a cis double
bond at carbon 15 of linoleoyl and gamma-linolenoyl groups attached
to the sn-1 position of glycerolipids.
- The enzyme is an omega desaturase, and determines the location of the
double bond by counting three carbons from the methyl end of the
fatty acid.
- It is non-specific with respect to the polar head group of the
glycerolipid. cf. EC 1.14.19.35.
|
| Cross-references |
|---|
| BRENDA | 1.14.19.36 |
| EC2PDB | 1.14.19.36 |
| ExplorEnz | 1.14.19.36 |
| PRIAM enzyme-specific profiles | 1.14.19.36 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.19.36 |
| IUBMB Enzyme Nomenclature | 1.14.19.36 |
| IntEnz | 1.14.19.36 |
| MEDLINE | Find literature relating to 1.14.19.36 |
| MetaCyc | 1.14.19.36 |
| Rhea expert-curated reactions | 1.14.19.36 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.14.19.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-
