Article
A monomer form of the glutathione S-transferase Y7F mutant from Schistosoma japonicum at acidic pH.
Biochemical and biophysical research communications - 30 Jan 2004
Andújar-Sánchez Montserrat, Clemente-Jimenez Josefa María, Rodriguez-Vico Felipe, Las Heras-Vazquez Francisco Javier, Jara-Pérez Vicente, Cámara-Artigas Ana
Abstract excerpt
Dissociation and unfolding of homodimeric glutathione S-transferase Y7F mutant from Schistosoma japonicum (SjGST-Y7F) were investigated at equilibrium using urea as denaturant. The conserved residue Tyr7 plays a central role in the catalytic mechanism and the mutation Tyr-Phe yields an inactive enzyme that is able to bind the substrate GSH with a higher binding constant than the wild type enzyme. Mutant SjGST-Y7F...
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