Cloned (Comment) | Organism |
---|---|
- |
Cucumis sativus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | lipid body | Cucumis sativus | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cucumis sativus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cotyledon | - |
Cucumis sativus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
linoleate + O2 | - |
Cucumis sativus | (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate | the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is 87:13 for the enzyme from cucumber cotyledons, and 84:16 for the recombinant enzyme. A linoleate 9-LOX preferentially oxygenates free fatty acids whereas a linoleate 13-LOX is capable of oxygenating triolein to significantly higher degrees in all positions of the triacylglycerol. For 9-LOXs, the carboxylate anion of the substrate may be the binding or recognition site within the catalytic pocket of the enzyme, whereas in the case of 13-LOXs the unpolar hydrophobic tail of the fatty acid may be orientated towards the catalytic pocket of the enzyme. This may explain why unpolar substrates, such as trilinolein, are preferred substrates for linoleate 13-LOXs | ? | |
additional information | oxygenation of triolein by lipid body LOX leads to a trihydroperoxy derivative | Cucumis sativus | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
triolein as substrate | Cucumis sativus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.6 | 8.5 | pH 5.6. about 50% of maximal activity, pH 8.5: about 70% of maximal activity | Cucumis sativus |