Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics
Por:
Valenzuela-Chavira, I., Contreras-Vergara, C.A., Arvizu-Flores, A.A., Serrano-Posada, H., Lopez-Zavala, A.A., García-Orozco, K.D., Hernandez-Paredes, J., Rudiño-Piñera, E., Stojanoff, V., Sotelo-Mundo, R.R., Islas-Osuna, M.A.
Publicada:
1 abr 2017
Resumen:
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.
Filiaciones:
Laboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo A.C. (CIAD), Hermosillo, Sonora, Mexico
Laboratorio de Genética Molecular de Plantas, Centro de Investigación en Alimentación y Desarrollo A.C. (CIAD), Hermosillo, Sonora, Mexico
Departamento de Ciencias Químico Biológicas, Universidad de Sonora, Hermosillo, Sonora, Mexico
CONACyT, Laboratorio de Bioingeniería, Universidad de Colima, Coquimatlán, Colima, Mexico
Departamento de Física, Universidad de Sonora, Hermosillo, Sonora, Mexico
Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología (IBT), Universidad Nacional Autónoma de México (UNAM), Cuernavaca, Morelos, Mexico
Brookhaven National Laboratory, Photon Science Directorate, Upton, NY, United States
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