Journal
BIOCHIMIE
Volume 135, Issue -, Pages 35-45Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2017.01.005
Keywords
Glutathione S-transferase; Tau class; Mango; Mangifera indica; Glutathione; S-hexyl glutathione; Detoxification; Crystal structure; Isothermal titration calorimetry
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Funding
- Mexico's National Research Council for Science and Technology [CONACYT CB-2012-178296]
- CONACYT [RET-I0007-2015-01/250973, INFR-2013-01-205617, INFR-2014-01-225455]
- LSBR
- NSLSII
- SMB
- SSRL under NIH-NIGMS [P41GM111244, P41GM103393]
- DOE BER [DE-SC0012704]
- DOE BES [DE-ACO2-76SF00515]
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We studied a mango glutathione S-transferase (GST) (Mangifera indica) bound to glutathione (GSH) and S-hexyl glutathione (GSX). This GST Tau class (MiGSTU) had a molecular mass of 25.5 kDa. MiGSTU Michaelis-Menten kinetic constants were determined for their substrates obtaining a Km, V-max and k(cat) for CDNB of 0.792 mM, 80.58 mM min (-1) and 68.49 s(-1) respectively and 0.693 mM, 105.32 mM min -1 and 89.57 s(-1), for reduced GSH respectively. MiGSTU had a micromolar affinity towards GSH (5.2 mu M) or GSX (7.8 mu M). The crystal structure of the MiGSTU in apo or bound to GSH or GSX generated a model that explains the thermodynamic signatures of binding and showed the importance of enthalpic-entropic compensation in ligand binding to Tau-class GST enzymes. (C) 2017 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
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