Glutathione S-transferases (GSTs) are one of the major families of detoxifying enzymes that detoxifies different chemical compounds including insecticides in different insect species. Among the GST subclasses, sigma GSTs are found to be the most abundant and conserved among different insect orders. These GSTs are found to play an important role in lipid peroxidation as well as detoxification. C...

A cluster of eight genes encoding glutathione transferases (GSTs) are located on division 33B of polytene chromosome arm 3R of the African malaria mosquito, Anopheles gambiae. This region of the genome contains a major 1,1,1-trichloro-2,2-bis-( p -chlorophenyl)ethane (DDT)-resistance locus, rtd1. These GSTs belong to the insect-specific Epsilon class and share between 22.6 and 65.2% identity at...

Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in det...

Glutathione S-transferases (GSTs) are widespread in Fasciola. hepatica parasite and sheep liver tissue. Study of GSTs inhibition assays in F. hepatica and sheep liver tissue are a priority of chemotherapeutic targets in parasitic liver diseases including human fascioliasis in Iran. In this research, the whole extract of F. hepatica and sheep liver tissues were purified and eluted for sodium dod...

The nitroaromatic explosive 2,4,6-trinitrotoluene (TNT) and the related 2,4-dinitrotoluene (DNT) are toxic environmental pollutants. The biotransformation and detoxication of these persistent compounds in higher organisms are of great significance from a health perspective as well as for the biotechnological challenge of bioremediation of contaminated soil. We demonstrate that different human g...

The glutathione transferases (GSTs) are one of the most important families of detoxifying enzymes in nature. The classic activity of the GSTs is conjugation of compounds with electrophilic centers to the tripeptide glutathione (GSH), but many other activities are now associated with GSTs, including steroid and leukotriene biosynthesis, peroxide degradation, double-bond cis-trans isomerization, ...

Background: Glutathione S-transferases (GSTs) are detoxifying enzymes that contribute to the glutathione-ascorbic acid (vitamin C) antioxidant cycle. Objective: The objective was to determine whether GST genotypes modify the association between dietary vitamin C and serum ascor-

The glutathione transferases (GSTs; also known as glutathione S-transferases) are major phase II detoxification enzymes found mainly in the cytosol. In addition to their role in catalysing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of other functions. They have peroxidase and isomerase activities, they can inhibit the Jun N-terminal ki...

Glutathione S-transferases (GSTs) play an important role in detoxification of various toxic compounds like carcinogens in cigarette smoke and tobacco by conjugating to toxic compounds and inactivating their hazardous effect. Variation in Glutathione S-Transferases (GSTs) genes may alter the catalytic efficiency of GST isoenzymes leading to potential increase in cancer susceptibility due to vari...

Parts of this thesis are based on a previous licentiate thesis v To the martyrs of APS attack, Peshawar vi vii Identification of new inhibitors for human hematopoietic prostaglandin D2 synthase among FDA-approved drugs and other compounds, Chem Biol Interact 229 (2015) 91-99. Overexpression of glutathione transferase E7 in Drosophila differentially impacts toxicity of organic isothiocyanates in...