Crystallographic and Thermodynamic Analysis of the Binding of S-Octylglutathione to the Tyr 7 to Phe Mutant of Glutathione S-Transferase from Schistosoma japonicum
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Andújar Sánchez, Montserrat![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
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Fecha
2005Resumen
Glutathione S-transferases are a family of multifunctional enzymes involved in the metabolism
of drugs and xenobiotics. Two tyrosine residues, Tyr 7 and Tyr 111, in the active site of the enzyme play
an important role in the binding and catalysis of substrate ligands. The crystal structures of Schistosoma
japonicum glutathione S-transferase tyrosine 7 to phenylalanine mutant [SjGST(Y7F)] in complex with
the substrate glutathione (GSH) and the competitive inhibitor S-octylglutathione (S-octyl-GSH) have been
obtained. These new structural data combined with fluorescence spectroscopy and thermodynamic data,
obtained by means of isothermal titration calorimetry, allow for detailed characterization of the ligandbinding
process. The binding of S-octyl-GSH to SjGST(Y7F) is enthalpically and entropically driven at
temperatures below 30 °C. The stoichiometry of the binding is one molecule of S-octyl-GSH per mutant
dimer, whereas shorter alkyl derivatives bind with a stoichiometry of tw...
Palabra/s clave
Glutathione S-Transferase
Mutant
Schistosoma japonicum
Crystallographic Analysis
Thermodynamic Analysis
Binding