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효소 Lipoxygenase의 신규기질 : Acylglycerol, acylethanolamide, lysophospholipids 및 phospholipids
황룡쌍,류희문,박천호,석대은 충남대학교 약학대학 의약품개발연구소 2007 藥學論文集 Vol.22 No.-
Lipoxygenase belongs to a diverse family of nonheme ferroproteins that oxygenate polyenoic fatty acids containing 1,4-pentadiene structure to form their corresponding hydroperoxy derivatives. Lipoxygenases (LOXs), widely distributed in animals and plants, have a key function in the formation of biologically active substances from pulyunsaturated fatty acids. Generally, free polyunsaturated fatty acids, liberated from membrane phospholipids via phospholipase-catalyzed hydrolysis, are used as substrates for LOXs. Although it is acknowledged that free polyunsaturated fatty acids are preferred to phospholipids or triglycerides as substrates, there have been recent reports that mammalian enzymes can oxidize certain phospholipids. Especially, reticulocyte LOX (15-LOX) leukocyte 15-LOX, leukocyte LOX (12-LOX) can oxygenate complex substrates such as phospholipids and biomembranes. In addition, acylglycerol and acylethanolamide are utilized by lipoxygeanse as well as cycoloxygenase; the latter enzyme contributes to generation of bioactive prostanoids derivative. Furthermore, lysophosphatidylcholine or lysophosphatidic acid containing linoleoyl or arachidonoyl moieties are known to be oxygenated by reticulocyte LOX, leukocyte 15-LOX or leukocyte-type 12-LOX; oxygenated lysophospholipids can play a carrier role in transporting oxygenated derivatives. Thus, the use of various lipid substrates as new substrates for lipoxygenase may extend the physiological roles of those lipids containing unsaturated fatty acyl chains.
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