Authors: Fereniki Perperopoulou Farid S Ataya Dalia Fouad Ajamaluddin Malik Hesham Mahmoud Saeed Nikolaos E Labrou
Publish Date: 2016/09/17
Volume: 74, Issue: 4, Pages: 459-472
Abstract
Glutathione transferase GST EC 25118 is a primary line of defense against toxicities of electrophile compounds and oxidative stress and therefore is involved in stressresponse and cell detoxification In the present study we investigated the catalytic and structural properties of the glutathione transferase GST isoenzyme P11 from Camelus dromedarius CdGSTP11 Recombinant CdGSTP11 was produced in Escherichia coli BL21DE3 and purified to electrophoretic homogeneity Kinetic analysis revealed that CdGSTP11 displays broad substrate specificity and shows high activity towards halogenated arylcompounds isothiocyanates and hydroperoxides Computation analysis and structural comparison of the catalytic and ligand binding sites of CdGSTP11 with other pi class GSTs allowed the identification of major structural variations that affect the active site pocket and the catalytic mechanism Affinity labeling and kinetic inhibition studies identified key regions that form the ligandinbinding site Lsite and gave further insights into the mechanism of nonsubstrate ligand recognition The results of the present study provide new information into camelid detoxifying mechanism and new knowledge into the diversity and complex enzymatic functions of GST superfamily
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