Determination of the Inhibitory Mechanism of Eugenyl Adamantate on 15-Lipoxygenase

Lipoxygenases are non-hem iron-containing proteins responsible for the peroxidation of the unsaturated lipids in animals and plants. The critical role of the enzymes in creating inflammations, sensitivities and some of the cancers has been demonstrated in mammalians. The study of mechanism details of these category of enzymes and the metabolism of their peroxide products as well as the synthesis of appropriates inhibitors is of great importance for the mentioned enzymes. In this article, the inhibitory mechanisms of eugenyl adamantate which is a new synthetic potent inhibitor of lipoxygenase is studied. The lipoxygenase activity of soybean 15-lipoxygenase in the presence of eugenyl adamantate was assayed by using two spectrophotometric the formation of conjugated dien in 235 nm and DMAB-MBTH peroxide in 592 nm. The experiments show that the mentioned compound decreases the lipoxygenase activity in two concentration ranges of 80-120 nM and 5-13 µM. The kinetic studies show the mixed inhibitory mechanism including the competitive and non-competitive for this compound. The kinetic studies show the mixed inhibitory mechanism for the compound.