Glutathione transferases are structural and functional outliers in the thioredoxin fold.

ABSTRACT: Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in detail, little else is known about the structural and functional relationships between different groupings of GSTs. Through a global analysis of sequence and structural similarity, it was determined that variation in the binding of glutathione between the two major subgroups of cytosolic (soluble) GSTs results in a different mode of glutathione activation. Additionally, the convergent features of glutat

SUBMITTER: Atkinson HJ 

PROVIDER: S-EPMC2778357 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature