A tale of plant Glutathione S-transferases: Since 1970

Abstract

Ubiquitously distributed multifunctional superfamily of Glutathione S-transferases (GST) generally constitute a dimeric enzymes and catalyse the conjugation of the thiol group of the glutathione (GSH) to diverse electrophilic centres on lipophilic molecules with the formation of rather less active end products. Besides their well investigated conjugation reaction for the detoxification of endogenous and xenobiotic compounds, they can also be involved in both GSH dependent peroxidation or isomerization reactions, and several other non-catalytic functions, like binding of non-substrate ligands, stress-induced signalling processes and preventing of apoptosis. Plant GSTs have been a focus of attention because of their roles in herbicide detoxification and today seven distinct classes of soluble (cytosolic) GSTs are presented as Phi, Tau, Theta, Zeta, Lambda, Dehydroascorbate reductases (DHARs) and Tetrachlorohydroquinone dehalogenase (TCHQD). While GSTs show overall sequence diversification within and between classes, they retain a high level of three-dimensional structure conservation over long evolutionary periods. In this review mainly the soluble plant GSTs will be considered by giving attention to their structures, subcellular localizations, genomic organizations, catalytic/noncatalytic functions, and comparisons given with respect to their mammalian counterparts where necessary.