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Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.


ABSTRACT: 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, Vmax and kcat 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 ?M) or GSX (7.8 ?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.

SUBMITTER: Valenzuela-Chavira I 

PROVIDER: S-EPMC5346462 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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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 K<sub>m</sub>, V<sub>max</sub> and k<sub>cat</sub> for CDNB of 0.792 mM, 80.58 mM min<sup>-1</sup> and 68.49 s<sup>-1</sup> respectively and 0.693 mM, 105.32 mM min<sup>-1</sup> and 89.57 s<sup>-1</sup>, for reduced GSH  ...[more]

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