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

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 m, 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 mM) or GSX (7.8 mM). As a result, 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.
Authors:
 [1] ;  [1] ;  [2] ; ORCiD logo [3] ;  [2] ;  [1] ;  [4] ;  [5] ;  [6] ;  [1] ;  [1]
  1. Centro de Investigacion en Alimentacion y Desarrollo, Sonora (Mexico)
  2. Univ. de Sonora, Sonora (Mexico)
  3. Univ. de Colima, Colima (Mexico)
  4. Centro de Investigacion en Alimentacion y Desarrollo, Sonora (Mexico); Univ. de Sonora, Sonora (Mexico)
  5. Univ. Nacional Autonoma de Mexico (UNAM), Morelos (Mexico)
  6. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
Report Number(s):
BNL-203470-2018-JAAM
Journal ID: ISSN 0300-9084
Grant/Contract Number:
SC0012704
Type:
Accepted Manuscript
Journal Name:
Biochimie
Additional Journal Information:
Journal Volume: 135; Journal Issue: C; Journal ID: ISSN 0300-9084
Publisher:
Elsevier
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; Glutathione S-transferase; Tau class; Mango; Mangifera indica; Glutathione; S-hexyl glutathione; Detoxification; Crystal structure; Isothermal titration calorimetry
OSTI Identifier:
1435731
Alternate Identifier(s):
OSTI ID: 1414338