Linoleate 10R-lipoxygenase (EC 1.13.11.62, 10R-DOX, (10R)-dioxygenase, 10R-dioxygenase) is an enzyme with systematic name linoleate:oxygen (10R)-oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
| Linoleate 10R-lipoxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.62 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- linoleate + O2 (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
Linoleate 10R-lipoxygenase is involved in biosynthesis of oxylipins.
- ^ Garscha U, Oliw EH (May 2009). “Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis oF (10R)-dioxygenase with epoxyalcohol synthase activity”. The Journal of Biological Chemistry. 284 (20): 13755–65. doi:10.1074/jbc.M808665200. PMC 2679477. PMID 19289462.
- ^ Jernerén F, Garscha U, Hoffmann I, Hamberg M, Oliw EH (April 2010). “Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus”. Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids. 1801 (4): 503–7. doi:10.1016/j.bbalip.2009.12.012. PMID 20045744.
- Linoleate+10R-lipoxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
