Linoleate 8R-lipoxygenase

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Linoleate 8R-lipoxygenase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Linoleate 8R-lipoxygenase (EC, 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.


  1. ^ Brodhun F, Göbel C, Hornung E, Feussner I (May 2009). "Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450". The Journal of Biological Chemistry. 284 (18): 11792–805. doi:10.1074/jbc.M809152200. PMC 2673248Freely accessible. PMID 19286665. 
  2. ^ Hamberg M, Zhang LY, Brodowsky ID, Oliw EH (February 1994). "Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions". Archives of Biochemistry and Biophysics. 309 (1): 77–80. doi:10.1006/abbi.1994.1087. PMID 8117115. 
  3. ^ Garscha U, Oliw E (September 2008). "Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase". Biochemical and Biophysical Research Communications. 373 (4): 579–83. doi:10.1016/j.bbrc.2008.06.060. PMID 18586008. 
  4. ^ Su C, Oliw EH (June 1996). "Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein". The Journal of Biological Chemistry. 271 (24): 14112–8. doi:10.1074/jbc.271.24.14112. PMID 8662736. 

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