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Site‐directed mutagenesis of the Proteus mirabilis glutathione transferase B1‐1 G‐site
Author(s) -
Casalone Enrico,
Allocati Nerino,
Ceccarelli Ilaria,
Rossjohn Jamie,
Parker Michael W,
Di Ilio Carmine
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00080-5
Subject(s) - glutathione , mutagenesis , site directed mutagenesis , biochemistry , chemistry , transferase , glutathione s transferase , cysteine , proteus mirabilis , residue (chemistry) , stereochemistry , enzyme , mutation , escherichia coli , gene , mutant
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.