Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics

Ignacio Valenzuela-Chavira; Carmen A. Contreras-Vergara; Aldo A. Arvizu-Flores; Hugo Serrano-Posada; Alonso A. Lopez-Zavala; Karina D. García-Orozco; Javier Hernandez-Paredes; Enrique Rudiño-Piñera; Vivian Stojanoff; Rogerio R. Sotelo-Mundo; Maria A. Islas-Osuna

doi:10.1016/j.biochi.2017.01.005

Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics

Ignacio Valenzuela-Chavira, Carmen A. Contreras-Vergara, Aldo A. Arvizu-Flores, Hugo Serrano-Posada, Alonso A. Lopez-Zavala, Karina D. García-Orozco, Javier Hernandez-Paredes, Enrique Rudiño-Piñera, Vivian Stojanoff, Rogerio R. Sotelo-Mundo, Maria A. Islas-Osuna

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

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 K_m, 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 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.

Original language	English
Pages (from-to)	35-45
Number of pages	11
Journal	Biochimie
Volume	135
DOIs	https://doi.org/10.1016/j.biochi.2017.01.005
State	Published - 1 Apr 2017
Externally published	Yes

Keywords

Crystal structure
Detoxification
Glutathione
Glutathione S-transferase
Isothermal titration calorimetry
Mangifera indica
Mango
S-hexyl glutathione
Tau class

Access to Document

10.1016/j.biochi.2017.01.005

Cite this

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. (2017). Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics. Biochimie, 135, 35-45. https://doi.org/10.1016/j.biochi.2017.01.005

@article{8e18dbcc954c4fbaac922a4ca844a93b,

title = "Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics",

abstract = "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.",

keywords = "Crystal structure, Detoxification, Glutathione, Glutathione S-transferase, Isothermal titration calorimetry, Mangifera indica, Mango, S-hexyl glutathione, Tau class",

author = "Ignacio Valenzuela-Chavira and Contreras-Vergara, {Carmen A.} and Arvizu-Flores, {Aldo A.} and Hugo Serrano-Posada and Lopez-Zavala, {Alonso A.} and Garc{\'i}a-Orozco, {Karina D.} and Javier Hernandez-Paredes and Enrique Rudi{\~n}o-Pi{\~n}era and Vivian Stojanoff and Sotelo-Mundo, {Rogerio R.} and Islas-Osuna, {Maria A.}",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier B.V. and Soci{\'e}t{\'e} Fran{\c c}aise de Biochimie et Biologie Mol{\'e}culaire (SFBBM)",

year = "2017",

month = apr,

day = "1",

doi = "10.1016/j.biochi.2017.01.005",

language = "English",

volume = "135",

pages = "35--45",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier",

}

Valenzuela-Chavira, I, Contreras-Vergara, CA, Arvizu-Flores, AA, Serrano-Posada, H, Lopez-Zavala, AA, García-Orozco, KD, Hernandez-Paredes, J, Rudiño-Piñera, E, Stojanoff, V, Sotelo-Mundo, RR & Islas-Osuna, MA 2017, 'Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics', Biochimie, vol. 135, pp. 35-45. https://doi.org/10.1016/j.biochi.2017.01.005

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.

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 - Article

C2 - 28104507

AN - SCOPUS:85009985957

SN - 0300-9084

VL - 135

SP - 35

EP - 45

JO - Biochimie

JF - Biochimie

ER -

Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics

Abstract

Keywords

Access to Document

Fingerprint

Cite this