TY - JOUR
T1 - Insights into ligand binding to a glutathione S-transferase from mango
T2 - Structure, thermodynamics and kinetics
AU - Valenzuela-Chavira, Ignacio
AU - Contreras-Vergara, Carmen A.
AU - Arvizu-Flores, Aldo A.
AU - Serrano-Posada, Hugo
AU - Lopez-Zavala, Alonso A.
AU - García-Orozco, Karina D.
AU - Hernandez-Paredes, Javier
AU - Rudiño-Piñera, Enrique
AU - Stojanoff, Vivian
AU - Sotelo-Mundo, Rogerio R.
AU - Islas-Osuna, Maria A.
N1 - Publisher Copyright:
© 2017 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)
PY - 2017/4/1
Y1 - 2017/4/1
N2 - 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.
AB - 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.
KW - Crystal structure
KW - Detoxification
KW - Glutathione
KW - Glutathione S-transferase
KW - Isothermal titration calorimetry
KW - Mangifera indica
KW - Mango
KW - S-hexyl glutathione
KW - Tau class
UR - http://www.scopus.com/inward/record.url?scp=85009985957&partnerID=8YFLogxK
U2 - 10.1016/j.biochi.2017.01.005
DO - 10.1016/j.biochi.2017.01.005
M3 - Artículo
SN - 0300-9084
VL - 135
SP - 35
EP - 45
JO - Biochimie
JF - Biochimie
ER -