Shifting substrate specificity of human glutathione transferase (from class Pi to class Alpha) by a single point mutation

Marzia Nuccetelli, Anna P. Mazzetti, Jamie Rossjohn, Michael W. Parker, Philip Board, Anna M. Caccuri, Giorgio Federici, Giorgio Ricci, Mario Lo Bello

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18 Citations (Scopus)


Substrate selectivity, among glutathione transferase (GST) isoenzymes, appears to be determined by a few residues. As part of study to determine which residues are class-specific determinants, Tyr 108 (an important residue of the class Pi) has been changed to a valine, the structural equivalent of a class Alpha enzyme. Using a panel of selected substrates, 'diagnostic' for either class Pi or Alpha, it is shown here that this single mutation significantly alters the catalytic properties of the class Pi enzyme and shifts the substrate specificity of the enzyme toward that of the class Alpha enzyme.

Original languageEnglish
Pages (from-to)184-189
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 9 Nov 1998
Externally publishedYes

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