Linoleate 8R-lipoxygenase

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Linoleate 8R-lipoxygenase
Identifiers
EC number 1.13.11.60
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 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[edit]

  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. 

External links[edit]