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Literature summary for 1.13.11.12 extracted from
- On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1 (2010), J. Biol. Chem., 285, 39876-39887.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 13-hydroperoxy-linoleic acid | - |
Glycine max |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | the ferric enzyme is responsible for the catalytic activity | Glycine max | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Glycine max | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| linoleate + O2 | - |
Glycine max | (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate | - |
? | |
| additional information | LOX-1 barely reacts with (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate alone | Glycine max | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LOX-1 | - |
Glycine max |
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