EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.14.19.36 | a 1-gamma-linolenoyl 2-acyl-sn-glycerol 3-phosphate + 2 reduced ferredoxin + O2 + 2 H+ |
- |
Synechocystis sp. |
a 1-stearidonoyl 2-acyl-sn-glycerol 3-phosphate + 2 oxidized ferredoxin + 2 H2O |
- |
? |
| 1.14.19.36 | a 1-gamma-linolenoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ |
- |
Nostoc sp. |
a 1-stearidonoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
- |
? |
| 1.14.19.36 | a 1-linoleoyl 2-acyl-sn-glycerol 3-phosphate + 2 reduced ferredoxin + O2 + 2 H+ |
- |
Synechocystis sp. |
a 1-alpha-linolenoyl 2-acyl-sn-glycerol 3-phosphate + 2 oxidized ferredoxin + 2 H2O |
- |
? |
| 1.14.19.36 | a 1-linoleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ |
- |
Nostoc sp. |
a 1-alpha-linolenoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
- |
? |
| 1.14.19.36 | more |
enzyme FAD8 acts preferentially on fatty acids esterified to the sn-1 position of glycerolipids. This might explain why FAD8 acts poorly on 16:2 substrates (always in the sn-2 position) or the higher selectivity for phosphatidylglycerol (which contains 18:2 only in sn-1) |
Arabidopsis thaliana |
? |
- |
? |
| 1.14.19.36 | more |
enzyme FAD8 acts preferentially on fatty acids esterified to the sn-1 position of glycerolipids. This might explain why FAD8 acts poorly on 16:2 substrates (always in the sn-2 position) or the higher selectivity for phosphatidylglycerol (which contains 18:2 only in sn-1) |
Arabidopsis thaliana Col-0 |
? |
- |
? |
