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

Ignacio Valenzuela-Chavira, Carmen A. Contreras-Vergara, Aldo A. Arvizu-Flores, Hugo Serrano-Posada, Alonso A. Lopez-Zavala, Karina D. García-Orozco, Javier Hernandez-Paredes, Enrique Rudiño-Piñera, Vivian Stojanoff, Rogerio R. Sotelo-Mundo*, Maria A. Islas-Osuna

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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 μM) or GSX (7.8 μM). 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.

Original languageEnglish
Pages (from-to)35-45
Number of pages11
JournalBiochimie
Volume135
DOIs
StatePublished - 1 Apr 2017

Bibliographical note

Publisher Copyright:
© 2017 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)

Keywords

  • Crystal structure
  • Detoxification
  • Glutathione
  • Glutathione S-transferase
  • Isothermal titration calorimetry
  • Mangifera indica
  • Mango
  • S-hexyl glutathione
  • Tau class

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