Biology:Linoleate 8R-lipoxygenase

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Linoleate 8R-lipoxygenase
Identifiers
EC number1.13.11.60
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate

Linoleate 8R-lipoxygenase contains heme.

References

  1. "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. May 2009. doi:10.1074/jbc.M809152200. PMID 19286665. 
  2. "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. February 1994. doi:10.1006/abbi.1994.1087. PMID 8117115. 
  3. "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. September 2008. doi:10.1016/j.bbrc.2008.06.060. PMID 18586008. 
  4. "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. June 1996. doi:10.1074/jbc.271.24.14112. PMID 8662736. 

External links