title: Human cytosolic glutathione transferases: structure, function, and drug discovery.
abstract: Glutathione transferases (GSTs) are important detoxifying enzymes that catalyze the conjugation of electrophilic substrates to glutathione. In recent years, GSTs have been of great interest in pharmacology and drug development because of their involvement in many important biological processes such as steroid and prostaglandin biosynthesis, tyrosine catabolism, and cell apoptosis. This review describes crystal structures for cytosolic GSTs and correlates active-site features with enzyme functions (e.g., steroid synthesis, tyrosine degradation, and dehydroascorbate reduction) and substrate selectivity. Use of these crystal structures for the design of specific inhibitors for several GST enzymes is also discussed.
authors.affiliation: Division of Pharmaceutics, College of Pharmacy, Jinan University, Guangzhou, Guangdong, China. bj.wu@hotmail.com
authors.forename: Baojian
authors.initials: B
authors.lastname: Wu
authors.forename: Dong
authors.initials: D
authors.lastname: Dong
mesh_terms: D018360:Crystallography, X-Ray; D003600:Cytosol / Q000201:enzymology*; D055808:Drug Discovery; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D013329:Structure-Activity Relationship
chemical_list: D004791:Enzyme Inhibitors; D005982:Glutathione Transferase