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Abstract
Glutathione S-transferases (GSTs) are abundant proteins encoded by a highly divergent,
ancient gene family. Soluble GSTs form dimers, each subunit of which contains active
sites that bind glutathione and hydrophobic ligands. Plant GSTs attach glutathione
to electrophilic xenobiotics, which tags them for vacuolar sequestration. The role
of GSTs in metabolism is unclear, although their complex regulation by environmental
stimuli implies that they have important protective functions. Recent studies show
that GSTs catalyse glutathione-depend-ent isomerizations and the reduction of toxic
organic hydroperoxides. GSTs might also have non-catalytic roles as carriers for phytochemicals.