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PDBsum entry 5g5e
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References listed in PDB file
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Key reference
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Title
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Insights into ligand binding to a glutathione s-Transferase from mango: structure, Thermodynamics and kinetics.
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Authors
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I.Valenzuela-Chavira,
C.A.Contreras-Vergara,
A.A.Arvizu-Flores,
H.Serrano-Posada,
A.A.Lopez-Zavala,
K.D.García-Orozco,
J.Hernandez-Paredes,
E.Rudiño-Piñera,
V.Stojanoff,
R.R.Sotelo-Mundo,
M.A.Islas-Osuna.
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Ref.
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Biochimie, 2017,
135,
35-45.
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PubMed id
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Abstract
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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.
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