5g5e

Publication Abstract from PubMed

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 muM) or GSX (7.8 muM). 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.

Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.,Valenzuela-Chavira I, Contreras-Vergara CA, Arvizu-Flores AA, Serrano-Posada H, Lopez-Zavala AA, Garcia-Orozco KD, Hernandez-Paredes J, Rudino-Pinera E, Stojanoff V, Sotelo-Mundo RR, Islas-Osuna MA Biochimie. 2017 Jan 16. pii: S0300-9084(16)30283-8. doi:, 10.1016/j.biochi.2017.01.005. PMID:28104507^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.