Arachidonate 15-lipoxygenase
arachidonate 15-lipoxygenase | |||||||||
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Identifiers | |||||||||
EC number | 1.13.11.33 | ||||||||
CAS number | 82249-77-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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Arachidonate 15-lipoxygenase (EC 1.13.11.33), also known as 15-lipoxygenase and 15-LOX, is an enzyme in humans that consists of two subtypes, 15-lipoxygenase-1 (15-LOX-1) and 15-lipoxygenase-2 (15-LOX-2). Human 15-LOX-1 is responsible for the production of proinflammatory eoxin compounds from arachidonic acid (analogous to 5-LOX and leukotrienes) in eosinophils and mast cells.[1]
In enzymology, 15-LOX catalyzes the chemical reaction:
- arachidonate + O2 (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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1LOX.
References
- ↑ Feltenmark S, Gautam N, Brunnström A, Griffiths W, Backman L, Edenius C, Lindbom L, Björkholm M, Claesson HE (January 2008). "Eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in human eosinophils and mast cells". Proc. Natl. Acad. Sci. U.S.A. 105 (2): 680–685. doi:10.1073/pnas.0710127105. PMC 2206596. PMID 18184802.
- 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. doi:10.1016/0005-2760(89)90342-1. 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.
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