ALOX15

Arachidonate 15-lipoxygenase

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2ABT

Identifiers

Symbols

ALOX15 ; 12-LOX; 15-LOX-1; 15LOX-1

External IDs

OMIM: 152392 MGI: 87997 HomoloGene: 44935 IUPHAR: 1388 ChEMBL: 2903 GeneCards: ALOX15 Gene

EC number

1.13.11.31, 1.13.11.33

Gene ontology
Molecular function	• arachidonate 12-lipoxygenase activity • iron ion binding • protein binding • phosphatidylinositol-4,5-bisphosphate binding • arachidonate 15-lipoxygenase activity • eoxin A4 synthase activity
Cellular component	• lipid particle • cytosol • plasma membrane • membrane • extrinsic component of cytoplasmic side of plasma membrane
Biological process	• ossification • negative regulation of adaptive immune response • phosphatidylethanolamine biosynthetic process • leukotriene metabolic process • inflammatory response • positive regulation of cell-substrate adhesion • arachidonic acid metabolic process • lipoxygenase pathway • bone mineralization • positive regulation of actin filament polymerization • response to endoplasmic reticulum stress • regulation of peroxisome proliferator activated receptor signaling pathway • cellular response to interleukin-13 • wound healing • apoptotic cell clearance • small molecule metabolic process • hepoxilin biosynthetic process • oxidation-reduction process • positive regulation of ERK1 and ERK2 cascade • cellular response to calcium ion • regulation of engulfment of apoptotic cell • lipoxin A4 biosynthetic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
4.53 – 4.55 Mb

Chr 11:
70.34 – 70.35 Mb

PubMed search

Arachidonate 15-lipoxygenase is an enzyme that in humans is encoded by the ALOX15 gene.^[1] ALOX15, also termed 15-lipoxygenase-1 (15-LO-1 or 15-LOX-1), is distinguished from its related oxygenase, ALOX15B or 15-lipoxygenase-2. ALOX15 oxygenates arachidonic acid at either its 15 or 12 carbon position to form respectively 15-hydroperoxyicosatetraenoic acid and 12-hydroperoxyicosatetraenoic acid. 15-hydroperoxyicosatetraenoic (see 15-hydroxyicosatetraenoic acid) and 12-hydroperoxyicosatetraenoic (see 12-Hydroxyeicosatetraenoic acid) acids have intrinsic, biologically and medically significant bioactivities but are also further metabolized to a wide range of products whose activities extend far beyond their precursors.

References

↑ Funk CD, Funk LB, FitzGerald GA, Samuelsson B (May 1992). "Characterization of human 12-lipoxygenase genes". Proceedings of the National Academy of Sciences of the United States of America 89 (9): 3962–6. doi:10.1073/pnas.89.9.3962. PMC 525611. PMID 1570320.

Kelavkar U, Glasgow W, Eling TE (2003). "The effect of 15-lipoxygenase-1 expression on cancer cells". Current urology reports 3 (3): 207–14. doi:10.1007/s11934-002-0066-8. PMID 12084190.
Sigal E, Dicharry S, Highland E, Finkbeiner WE (1992). "Cloning of human airway 15-lipoxygenase: identity to the reticulocyte enzyme and expression in epithelium". Am. J. Physiol. 262 (4 Pt 1): L392–8. PMID 1566855.
Izumi T, Rådmark O, Jörnvall H, Samuelsson B (1992). "Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes". Eur. J. Biochem. 202 (3): 1231–8. doi:10.1111/j.1432-1033.1991.tb16495.x. PMID 1662607.
Conrad DJ, Kuhn H, Mulkins M et al. (1992). "Specific inflammatory cytokines regulate the expression of human monocyte 15-lipoxygenase". Proceedings of the National Academy of Sciences of the United States of America 89 (1): 217–21. doi:10.1073/pnas.89.1.217. PMC 48207. PMID 1729692.
Lei ZM, Rao CV (1992). "The expression of 15-lipoxygenase gene and the presence of functional enzyme in cytoplasm and nuclei of pregnancy human myometria". Endocrinology 130 (2): 861–70. doi:10.1210/en.130.2.861. PMID 1733732.
Izumi T, Rådmark O, Samuelsson B (1991). "Purification of 15-lipoxygenase from human leukocytes, evidence for the presence of isozymes". Adv. Prostaglandin Thromboxane Leukot. Res. 21A: 101–4. PMID 1825526.
Sloane DL, Leung R, Craik CS, Sigal E (1991). "A primary determinant for lipoxygenase positional specificity". Nature 354 (6349): 149–52. doi:10.1038/354149a0. PMID 1944593.
Nadel JA, Conrad DJ, Ueki IF et al. (1991). "Immunocytochemical localization of arachidonate 15-lipoxygenase in erythrocytes, leukocytes, and airway cells". J. Clin. Invest. 87 (4): 1139–45. doi:10.1172/JCI115110. PMC 295116. PMID 2010530.
Kroschwald P, Kroschwald A, Kühn H et al. (1989). "Occurrence of the erythroid cell specific arachidonate 15-lipoxygenase in human reticulocytes". Biochem. Biophys. Res. Commun. 160 (2): 954–60. doi:10.1016/0006-291X(89)92528-X. PMID 2719708.
Sigal E, Nadel JA (1989). "Arachidonic acid 15-lipoxygenase and airway epithelium. Biologic effects and enzyme purification". Am. Rev. Respir. Dis. 138 (6 Pt 2): S35–40. doi:10.1164/ajrccm/138.6_pt_2.s35. PMID 3202520.
Sigal E, Craik CS, Highland E et al. (1989). "Molecular cloning and primary structure of human 15-lipoxygenase". Biochem. Biophys. Res. Commun. 157 (2): 457–64. doi:10.1016/S0006-291X(88)80271-7. PMID 3202857.
Sigal E, Grunberger D, Craik CS et al. (1988). "Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases". J. Biol. Chem. 263 (11): 5328–32. PMID 3356688.
Nassar GM, Morrow JD, Roberts LJ et al. (1994). "Induction of 15-lipoxygenase by interleukin-13 in human blood monocytes". J. Biol. Chem. 269 (44): 27631–4. PMID 7961680.
Kritzik MR, Ziober AF, Dicharry S et al. (1997). "Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene". Biochim. Biophys. Acta 1352 (3): 267–81. doi:10.1016/s0167-4781(97)00005-5. PMID 9224951.
Brinckmann R, Schnurr K, Heydeck D et al. (1998). "Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme". Blood 91 (1): 64–74. PMID 9414270.
Kelavkar U, Wang S, Montero A et al. (1998). "Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes". Mol. Biol. Rep. 25 (3): 173–82. doi:10.1023/A:1006813009006. PMID 9700053.
Roy B, Cathcart MK (1998). "Induction of 15-lipoxygenase expression by IL-13 requires tyrosine phosphorylation of Jak2 and Tyk2 in human monocytes". J. Biol. Chem. 273 (48): 32023–9. doi:10.1074/jbc.273.48.32023. PMID 9822675.
Kratky D, Lass A, Abuja PM et al. (1999). "A sensitive chemiluminescence method to measure the lipoxygenase catalyzed oxygenation of complex substrates". Biochim. Biophys. Acta 1437 (1): 13–22. doi:10.1016/s0005-2760(98)00176-3. PMID 9931410.
Kelavkar UP, Badr KF (1999). "Effects of mutant p53 expression on human 15-lipoxygenase-promoter activity and murine 12/15-lipoxygenase gene expression: Evidence that 15-lipoxygenase is a mutator gene". Proceedings of the National Academy of Sciences of the United States of America 96 (8): 4378–83. doi:10.1073/pnas.96.8.4378. PMC 16340. PMID 10200270.

Oxidoreductases: monooxygenases (EC 1.13)

1.13.11: two atoms of oxygen

other dioxygenase: Catechol dioxygenase
Homogentisate 1,2-dioxygenase
Cysteine dioxygenase
4-Hydroxyphenylpyruvate dioxygenase
Indoleamine 2,3-dioxygenase

1.13.12: one atom of oxygen

Firefly luciferase

1.13.99: other

Inositol oxygenase

Biochemistry overview
Enzymes overview
By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

ALOX15

References

Further reading