Arachidonate 15-lipoxygenase

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arachidonate 15-lipoxygenase
EC number
CAS number 82249-77-2
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, an arachidonate 15-lipoxygenase (EC is an enzyme that catalyzes the chemical reaction

arachidonate + O2 \rightleftharpoons (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate

Thus, the two substrates of this enzyme are arachidonate and O2, whereas its product is (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is arachidonate:oxygen 15-oxidoreductase. Other names in common use include 15-lipoxygenase, linoleic acid omega6-lipoxygenase, and omega6 lipoxygenase. This enzyme participates in arachidonic acid metabolism and linoleic acid metabolism.

Structural studies[edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1LOX.


  • Bryant RW, Bailey JM, Schewe T, Rapoport SM (1982). "Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid". J. Biol. Chem. 257 (11): 6050–5. PMID 6804460. 
  • Narumiya S, Salmon JA (1982). "Arachidonic acid-15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes". Methods' Enzymol. Methods in Enzymology 86: 45–8. doi:10.1016/0076-6879(82)86166-1. ISBN 978-0-12-181986-6. PMID 6813644. 
  • Oliw EH, Sprecher H (1989). "Metabolism of polyunsaturated fatty acids by an (n - 6)-lipoxygenase associated with human ejaculates". Biochim. Biophys. Acta. 1002 (3): 283–91. PMID 2496760. 
  • B; Steczko, J; Dixon, JE; Hermodson, M; Yazdanparast, R; Axelrod, B (1987). "Primary structure of soybean lipoxygenase-1". J. Biol. Chem. 262 (21): 10080–5. PMID 3112136.