کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5509100 1538397 2017 34 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 135, April 2017, Pages 35-45
نویسندگان
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