TY - JOUR
T1 - Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
AU - Casalone, Enrico
AU - Allocati, Nerino
AU - Ceccarelli, Ilaria
AU - Michele Masulli, Masulli
AU - Rossjohn, Jamie
AU - Parker, Michael W.
AU - Di Ilio, Carmine
PY - 1998/2/20
Y1 - 1998/2/20
N2 - 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.
AB - 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.
KW - Glutathione transferase
KW - Proteus mirabilis
KW - Site-directed mutagenesis
UR - http://www.scopus.com/inward/record.url?scp=0032548807&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(98)00080-5
DO - 10.1016/S0014-5793(98)00080-5
M3 - Article
C2 - 9512342
AN - SCOPUS:0032548807
VL - 423
SP - 122
EP - 124
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -