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Functional analysis of the evolutionarily conserved proline 53 residue in Proteus mirabilis glutathione transferase B1‐1
Author(s) -
Allocati Nerino,
Casalone Enrico,
Masulli Michele,
Ceccarelli Ilaria,
Carletti Erminia,
Parker Michael W,
Di Ilio Carmine
Publication year - 1999
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(99)00147-7
Subject(s) - proteus mirabilis , residue (chemistry) , enzyme , serine , glutathione , transferase , biochemistry , proline , mutagenesis , chemistry , site directed mutagenesis , amino acid , biology , bacteria , mutant , escherichia coli , genetics , gene
The role of the evolutionarily conserved residue Pro‐53 in Proteus mirabilis glutathione transferase B1‐1 has been examined by replacing it with a serine residue using site‐directed mutagenesis. The effect of the replacement on the activity, thermal stability and antibiotic binding capacity of the enzyme was examined. The results presented support the view that Pro‐53 participates in the maintenance of the proper conformation of the enzyme fold rather than playing a direct role in the catalytic reaction. Furthermore, this residue appears to be an important determinant of the antibiotic binding to the enzyme. Experiments with wild type and mutated enzymes provide evidence that glutathione transferases may play an important role in antibiotic resistance exhibited by bacteria.