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Significance Lipoxygenases are lipid-peroxidizing enzymes that have been classified according to their reaction specificity. ALOX15 (12/15-lipoxygenase) has been implicated in inflammatory resolution via biosynthesis of antiinflammatory and proresolving lipoxins. We found that lower mammals including lower primates express arachidonic acid 12-lipoxygenating ALOX15 orthologs, whereas higher primates express 15-lipoxygenating enzymes. Gibbons constitute the missing link interconnecting 12- and 15-lipoxygenating ALOX15 orthologs. To explore the evolutionary driving force for this specificity alteration, we quantified the lipoxin synthase activity of 12- and 15-lipoxygenating ALOX15 orthologs and observed that the lipoxin synthase activities of 15-lipoxygenating enzymes were significantly higher. These results suggest an evolution of ALOX15 specificity, which optimizes the biosynthetic capacity for antiinflammatory and proresolving lipoxins.

Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins