A Model of Arachidonic Acid Binding for 15-Lipoxygenase

Autor: Elliott Sigal, Michelle F. Browner, Qing-Fen Gan
Rok vydání: 1997
Předmět:
Zdroj: Advances in Experimental Medicine and Biology ISBN: 9781489918123
DOI: 10.1007/978-1-4899-1810-9_96
Popis: 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
Databáze: OpenAIRE