Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site

In order to investigate the roles of near N-terminus Tyr, Cys, and Ser residues in the activity of bacterial glutathione transferase (GSTB1-1) site-directed mutagenesis was used to replace the following residues: Tyr-4, Tyr-5, Ser-9, Cys-10, Ser-11, and Ser-13, The results presented here show that, unlike all other alpha, mu, pi, theta and sigma classes of glutathione transferases so far investigated, GSTB1-1 does not utilise any Tyr, Ser or Cys residue to activate glutathione, These results also suggest that the bacterial glutathione transferases mag require classification into their own class, (C) 1998 Federation of European Biochemical Societies.