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ALOX15
ALOX15 (also termed arachidonate 15-lipoxygenase, 15-lipoxygenase-1, 15-LO-1, 15-LOX-1) is an polyunsaturated fatty acid-metabolizing enzyme that in humans is encoded by the ALOX15 gene located on chromosome 17p13.3. The 11 kilobase pair gene consists of 14 exons and 13 introns coding for a 75 kiloDalton protein composed of 662 amino acids. 15-LO is distinguished from another human 15-lipoxygenase enzyme, ALOX15B (15-lipoxygenase-2).〔Gene. 2015 Nov 15;573(1):1-32. doi: 10.1016/j.gene.2015.07.073. Epub 2015 Jul 26.Review〕 Orthologs of ALOX15, termed Alox15, are widely distributed in animal and plant species.
== Nomenclature ==
Human ALOX15 was initially named arachidonate 15-lipoxygenase or 15-lipoxygenase but subsequent studies uncovered a second human enzyme with 15-lipoxygenase activity as well as various non-human mammalian that were closely related to and therefore orthologs of human ALOX15 but nonetheless possess 12-lipoxygenase rather than 15-lipoxygenase activity. Consequently, human ALOX15 is now referred to as arachidonate-15-lipoxygenase-1, 15-lipoxygenase-1, 15-LOX-1, 15-LO-1, human 12/15-lipoxygenase, leukocyte-type arachidonate 12-lipoxygenase, or arachidonate omega-6 lipoxygenase; the second discovered human 15-lipoxygenase, a product of the ALOX15B gene, is termed ALOX15B, arachidonate 15-lipoxygenase 2, 15-lipoxygenase-2, 15-LOX-2, 15-LO-2, arachidonate 15-lipoxygenase type II, arachidonate 15-lipoxygenase, second type, and arachidonate 15-lipoxygenase; and mouse, rat, and rabbit rodent orthologs of human ALOX15, which share 74-81% amino acid identity with the human enzyme, are commonly termed Alox15, 12/15-lipoxygenase (i.e. 12/15-LOX, and 12/15-LO).〔〔Gene. 2015 Nov 15;573(1):1-32. doi: 10.1016/j.gene.2015.07.073. Epub 2015 Jul 26.〕
Human 15-LOX-1 (ALOX15) and 15-LOX-2 ALOX15B genes are located on chromosome 17; their product proteins have an amino acid sequence identity of only ~38%, differ in the polyunsaturated fatty acids that they prefer as substrates, and exhibit different product profiles when acting on the same substrates.〔Gene. 2015 Nov 15;573(1):1-32. doi: 10.1016/j.gene.2015.07.073. Epub 2015 Jul 26.〕
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