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《Journal of Chengdu University(Natural Science Edition)》 2006-01
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Structure and Catalytic Mechanism of the Glutathione Transferases

YANG Hailing,NIE Lijia,ZHU Shenggeng,ZHOU Xianwan(College of Life Sciences,Peking University,Beijing 100871,China)  
The glutathione S-transferases(GST) are a supergene family of dimeric enzymes that catalyse the conjugation of glutathione(GSH) to a variety of electrophiles,including arene oxides,unsaturated carbonyls,organic halides and other substrates.Their importance is suggested by the finding that GST enzymes are expressed in probably all life forms.Since the first half of last decade scientists have been focusing on the elucidation of the three-dimensional structures of several cytosolic isoenzymes.The structural information has had a profound impact on our understanding of the catalytic mechanisms of the glutathione transferases,the evolution of the protein fold,and the molecular basis for their participation in the detoxification of endogenous and xenobiotic electrophiles.The purpose of this review is to illustrate how the knowledge of the three-dimensional structures has influenced current ideas on the evolution and function of these enzymes in biological systems.
【Fund】: 国家海洋836项目资助(819-04-02)
【CateGory Index】: Q55
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