Class-Pi of glutathione s-transferases (GST-Pi) is the specific form of GSTs that are known to participate particularly in the mechanisms of resistance to drugs and carcinogens. This class of the enzyme is referred to as class-P or class-Pi or class π. The accepted terminology in this review article is class-Pi. In this article following a brief description of identified molecular forms of GSTs...

In the present paper, we report a novel class of GSTs (glutathione transferases), called the Chi class, originating from cyanobacteria and with properties not observed previously in prokaryotic enzymes. GSTs constitute a widespread multifunctional group of proteins, of which mammalian enzymes are the best characterized. Although GSTs have their origin in prokaryotes, few bacterial representativ...

The evolution of resistance by an insect to an insecticide may involve several mechanisms. Many studies have shown that insecticide-resistant insects have elevated levels of glutathione S-transferases activity in crude homogenates, which suggests a role for GSTs in resistance. This prompted us to select the GSTs from H.armigera, L.lineolaris and M.sexta due to their economic importance. The 3D ...

Glutathione-S-transferases (GSTs) constitute a multifunctional family of dimeric and cytosolic enzymes which play an important role in biotransformation of tissues from oxidative stress. They catalyze the conjugation of intracellular glutathione with chemicals, that possess an electrophilic centre to facilitate their metabolism and elimination through mercapturic acid pathway. Acrylamide, a kno...

glutathione s-transferases (gsts) are encoded by a superfamily of genes and play a role in the detoxification of potential carcinogens. the human gsts are divided into four classes: alpha, mu, pi and theta. previous studies indicated that the absence of the glutathione s-transferase m1 (gstm1) protein correlated with an increased risk of developing some types of cancers. association between spe...

The glutathione S-transferases (GSTs) are a family of ubiquitously expressed polymorphic enzymes important for detoxifying endogenous and exogenous compounds. In addition to their classic activity of detoxification by conjugation of compounds with glutathione, many other functions are now found to be associated with GSTs. The associations between GST polymorphisms/functions and human disease su...

Glutathione S-transferases (GSTs) are multifunctional enzymes that are involved in the metabolism of endogenous and exogenous compounds and are related to insecticide resistance. The purpose of this study was to provide new information on the molecular characteristics and the positive selection of locust GSTs. Based on the transcriptome database, we sequenced 28 cytosolic GSTs and 4 microsomal ...

Glutathione transferases (GSTs) are a superfamily of enzymes which have in common the ability to catalyze nucleophilic addition thiol group reduced glutathione (GSH) onto electrophilic and hydrophobic substrates. This conjugation reaction, occurs spontaneously but is dramatically accelerated by enzyme, protects cells against damages caused harmful molecules. With some exceptions, GSTs catalytic...

Glutathione S-transferases (GSTs) are a diverse family of phase II detoxification enzymes found in almost all organisms. Besides playing a major role in the detoxification of xenobiotic and toxic compounds, GSTs are also involved in the regulation of mitogen activated protein (MAP) kinase signal transduction by interaction with proteins in the pathway. An in vitro study was performed for Theta,...

Selection of a laboratory colony of the brown planthopper Nilaparvata lugens with the pyrethroids permethrin and lambda-cyhalothrin increased its resistance to both insecticides. Biochemical analysis and synergistic studies with metabolic inhibitors indicated that elevated glutathione S-transferases (GSTs) with a predominant peroxidase activity conferred resistance to both pyrethroids, whereas ...