||This article includes a list of references, related reading or external links, but its sources remain unclear because it lacks inline citations. (July 2014)|
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
- arachidonate + O2 (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
Thus, the two substrates of this enzyme are arachidonate and oxygen, whereas its product is (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-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 12-oxidoreductase. Other names in common use include Delta12-lipoxygenase, 12-lipoxygenase, 12Delta-lipoxygenase, C-12 lipoxygenase, 12S-lipoxygenase, leukotriene A4 synthase, and LTA4 synthase. This enzyme participates in arachidonic acid metabolism. At least one compound, 3-methoxytropolone is known to inhibit this enzyme.
- Hamberg M, Samuelsson B (1974). "Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets". Proc. Natl. Acad. Sci. U.S.A. 71 (9): 3400–4. doi:10.1073/pnas.71.9.3400. PMC 433780. PMID 4215079.
- Nugteren DH (1975). "Arachidonate lipoxygenase in blood platelets". Biochim. Biophys. Acta. 380 (2): 299–307. doi:10.1016/0005-2760(75)90016-8. PMID 804329.
- Wallach DP, Brown VR (1981). "A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases". Biochim. Biophys. Acta. 663 (2): 361–72. PMID 6783111.