Format

Send to

Choose Destination
Drug Metab Rev. 2011 May;43(2):138-51. doi: 10.3109/03602532.2011.558093. Epub 2011 Mar 23.

Glutathione transferases: a structural perspective.

Author information

1
School of Chemistry, University of Wollongong, Wollongong, Australia. aarono@uow.edu.au

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.

PMID:
21428697
DOI:
10.3109/03602532.2011.558093
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Taylor & Francis
Loading ...
Support Center