The linoleyl alcohol oxidation catalyzed by potato tuber 5-lipoxygenase was found to be efficiently inhibited by stable nitroxyl radicals: 1-oxyl-2,2,6,6-tetramethylpiperidin-4-yl 1-bicyclo[2,2,2]octane-1-carboxylate, 1-adamantylacetate, dodecanoate, and octadecanoate. The dependence of apparent IC50 values on the rotational correlation times of times of 4-hydroxy-1-oxyl-2,2,6,6-tetramethylpiperidine and its derivatives in model micellar systems was analyzed. The inhibition mechanism was proposed; it involves the interaction of hydrophobic nitroxyl radical with the intermediate radical enzyme-substrate complex.
Lipoxygenases (LOs) are known as one of the enzymes of lipid peroxidation. The majority of LOs are soluble enzymes and have affi nity to membranes. The enzyme translocation from a cytosol to a membrane surface is one of the stages of regulation of the amount of LO catalysis products in the cell. A sorption to the membrane surface is described for most LOs from plant and animal sources. This review presents the data about regulation of the LO activity by the lipid compounds-both natural and chemically modifi ed. Lipids might regulate the LO activity through: protein-lipid interactions of C2 domain with the membrane, changes in the enzyme affi nity, the LOs translocation, allosteric regulation, increase in the selectivity towards substrates. The regulatory effect of active compound on the enzyme activity depends on the lipophilicity of effectors. Considering the LO activity it is necessary to take into account the enzyme microenvironment and its infl uence on the range of the LO products.
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