Linoleate 8R-lipoxygenase
Linoleate 8R-lipoxygenase (EC 1.13.11.60, linoleic acid 8R-dioxygenase, 5,8-LDS (bifunctional enzyme), 7,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 7,8-linoleate diol synthase (bifunctional enzyme), PpoA) is an enzyme with systematic name linoleate:oxygen (8R)-oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
- linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Linoleate 8R-lipoxygenase contains heme.
References
- ↑ Brodhun, F., Gobel, C., Hornung, E. and Feussner, I. (2009). "Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450". J. Biol. Chem. 284 (18): 11792–11805. doi:10.1074/jbc.M809152200. PMC 2673248. PMID 19286665.
- ↑ Hamberg, M., Zhang, L.-Y., Brodowsky, I.D. and Oliw, E.H. (1994). "Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions". Arch. Biochem. Biophys. 309: 77–80. doi:10.1006/abbi.1994.1087. PMID 8117115.
- ↑ Garscha, U. and Oliw, E. (2008). "Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase". Biochem. Biophys. Res. Commun. 373 (4): 579–583. doi:10.1016/j.bbrc.2008.06.060. PMID 18586008.
- ↑ Su, C. and Oliw, E.H. (1996). "Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein". J. Biol. Chem. 271: 14112–14118. doi:10.1074/jbc.271.24.14112. PMID 8662736.
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