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 residue s: Tyr-4, Tyr-5, Ser-9, Cys-10, Ser-11, and Ser-13, The results presen ted here show that, unlike all other alpha, mu, pi, theta and sigma cl asses of glutathione transferases so far investigated, GSTB1-1 does no t utilise any Tyr, Ser or Cys residue to activate glutathione, These r esults also suggest that the bacterial glutathione transferases mag re quire classification into their own class, (C) 1998 Federation of Euro pean Biochemical Societies.