Glutathione S-Transferase Pi Has at Least Three Distinguishable Xenobiotic Substrate Sites Close to Its Glutathione-binding Site
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منابع مشابه
Class-Pi of Glutathione S-Transferases
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...
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BACKGROUND Glutathione (GSH) is one of the most important agents of the antioxidant defense system of the cell because, in conjunction with the enzymes glutathione peroxidase (GSH-Px) and glutathione S transferase pi (GSTpi), it plays a central role in the detoxification and biotransformation of chemotherapeutic drugs. This study evaluated the expression of GSH and the GSH-Px and GSTpi enzymes ...
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Equine liver glutathione S-transferase has been shown to consist of two identical subunits of apparent Mr 25,500 and a pl of 8.9. Kinetic data at pH 6.5 with 1-chloro-2,4-dinitrobenzene as a substrate suggests a random rapid-equilibrium mechanism, which is supported by inhibition studies using glutathione analogues. S-(p-Bromobenzyl)glutathione and the corresponding N alpha-, CGlu- and CGly-sub...
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The glutathione transferases (EC 2.5.1.18) (GSTs) are a family of enzymes involved in the mechanism of cellular detoxification. They catalyze the nucleophilic attack of glutathione on the electrophilic centre of a number of toxic compounds. The cytosolic enzymes have two active sites per dimmer which behave independently of one another. The homodimeric (26 kDa per subunit) glutathione S-transfe...
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The reversibility of the conjugation reaction of the diuretic drug ethacrynic acid (EA), an a,~-unsaturated ketone, with glutathione and glutathione S-transferase PI-1 (GST PI-I) has been studied. When the glutathione conjugate of EA was incubated with a 5-fold molar excess of Nacetyi-L-cysteine or GST PI-I, a time-dependent transfer of EA to N-acetyI-L-cysteine or GST PI-1 was observed. With i...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m407445200