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Literature summary for 1.13.11.58 extracted from
- Dual positional and stereospecificity of lipoxygenase isoenzymes from germinating barley (green malt): biotransformation of free and esterified linoleic acid (2006), J. Agric. Food Chem., 54, 946-955.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hordeum vulgare | P29114 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Hordeum vulgare |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| linoleate + O2 | low catalytic activity with complex substrates as compared to free linoleic acid. Residual relative activities lower than 1% with the substrates dilinolein, trilinolein, and 1-palmitoyl-2-linoleoyl-glycero-3-phosphocholine and with extracted lipids from malt confirm this supposition. However, LOX1 catalyzes HPODE formation from PamLinGroPCho with high regioselectivity (9-hydroperoxy-(10E,12Z)-octadecadienoate:13-hydroperoxy-(10E,12Z)-octadecadienoate) and high (9S)-hydroperoxy-(10E,12Z)-octadecadienoate stereoselectivity (S:R) (92:8) | Hordeum vulgare | (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LOX1 | - |
Hordeum vulgare |
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Release 2023.1 (January 2023)
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