Glutathione transferases: a structural perspective

Abstract

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.

Keywords::

• Glutathione transferase
• GST
• structure
• function
• catalytic mechanism

Acknowledgment

The author thanks Prof. Xinhua Ji for providing the coordinates of the hGSTA3-3/Δ⁵-androstene-3,17-dione model.

Declaration of interest

Aaron Oakley is the recipient of an Australian Research Council Future Fellowship (project number FT0990287).