| Summary: | The microsomal glutathione S-transferases (GST, EC 2.5.1.18) constitute a group of phase II detoxification enzymes present in eukaryotic cells and prokaryotic organisms. They play significant roles in defense against carcinogenic, toxic, and pharmacologically active electrophilic compounds. The microsomal glutathione S-transferase is a homotrimeric, membrane-bound enzyme, that catalyzes conjugation of electrophilic compounds with glutathione and reduction of lipid hydroperoxides. Peroxidase activity may be of importance for protection against lipid peroxidation under conditions of oxidative stress. A number of biochemical approaches have been used to study the properties of MGST, including enzymatic activity, sub-cellular distribution, substrate specificity, and proteins structure. MGST is considered a member of the MAPEG (membrane- associated proteins in eicosanoid and glutathione metabolism) superfamily of structurally and phylogeneticaily related enzymes, including MGST 1, MGST 2, MGST3, microsomal Ya-GST, MGST 1 Like 1, 5-lipoxygenase activating protein, and leukotriene C4 synthase. Enzymes in this superfamily are involved in detoxification, protection from oxidative stress, and synthesis of prostaglandin E and cysteinyl leukotrienes. On the basis of understanding funcitons MGST is possible...
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