Abstract
Mammalian lipoxygenases have been implicated in the pathogenesis of various inflammatory conditions such as arthritis, psoriasis and bronchial asthma.1, 2 There is also evidence that 15-lipoxygenase may play a role in the progression of atherosclerosis. Lipoxygenases catalyze the stereo-specific oxygenation of fatty acids containing l,4-cis, cis-pentadiene. Three distinct mammalian lipoxygenase enzymes have been characterized, 5-, 12- and 15-lipoxygenases, named for their positional specificity on arachidonic acid. Mammalian 15-lipoxygenase has dual positional specificity; oxygenation of arachidonic acid produces two chiral products, 15(S)-hydroxyeicosatetraenoic acid (HETE) and 12(S)-HETE. It has been suggested that the positional specificity of mammalian 15-lipoxygenase is affected by the alignment of a doubly ailylic methylene carbon with the catalytic iron of the enzyme.3
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