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

Enrico Casalone, Nerino Allocati, Ilaria Ceccarelli, Masulli Michele Masulli, Jamie Rossjohn, Michael W. Parker, Carmine Di Ilio

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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 may require classification into their own class.

Original languageEnglish
Pages (from-to)122-124
Number of pages3
JournalFEBS Letters
Issue number2
Publication statusPublished - 20 Feb 1998
Externally publishedYes


  • Glutathione transferase
  • Proteus mirabilis
  • Site-directed mutagenesis

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