Characterization and functional analysis of a recombinant tau class glutathione transferase GmGSTU2-2 from Glycine max.

摘要: The plant tau class glutathione transferases (GSTs) perform diverse catalytic as well non-catalytic roles in detoxification of xenobiotics, prevention oxidative damage and endogenous metabolism. In the present work, isoenzyme GSTU2-2 from Glycine max (GmGSTU2-2) was characterized. Gene expression analysis GmGSTU2 suggested a highly specific selective induction pattern to osmotic stresses, indicating that gene is controlled by mechanism. Purified, recombinant GmGSTU2-2 shown exhibit wide-range specificity towards xenobiotic compounds ligand-binding properties, suggesting could provide flexibility numerous metabolic conditions. Homology modeling phylogenetic ligand binding sites are conserved compared other GSTs. Structural identified key amino acid residues hydrophobic site provided insights into substrate this enzyme. results established participates broad network regulatory functions involved stress response.