School of Chemistry, University of Wollongong, Wollongong, Australia.
Drug Metab Rev. 2011 May;43(2):138-51. doi: 10.3109/03602532.2011.558093. Epub 2011 Mar 23.
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, dehydroascorbate reduction, Michael addition, and noncatalytic "ligandin" activity (ligand binding and transport). Since the first GST structure was determined in 1991, there has been an explosion in structural data across GSTs of all three families: the cytosolic GSTs, the mitochondrial GSTs, and the membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG family). In this review, the major insights into GST structure and function will be discussed.
谷胱甘肽转移酶（GSTs）是自然界中最重要的解毒酶家族之一。GSTs 的经典活性是将具有亲电中心的化合物与三肽谷胱甘肽（GSH）缀合，但现在许多其他活性也与 GSTs 相关，包括甾体和白三烯生物合成、过氧化物降解、双键顺反异构化、脱氢抗坏血酸还原、迈克尔加成和非催化“配体结合”活性（配体结合和运输）。自 1991 年首次确定 GST 结构以来，所有三种家族的 GST 的结构数据都呈爆炸式增长：细胞溶质 GSTs、线粒体 GSTs 和类二十烷酸和谷胱甘肽代谢中的膜相关蛋白（MAPEG 家族）。在这篇综述中，将讨论 GST 结构和功能的主要见解。
