Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.

@article{Hsu2009ContributionOS,
  title={Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.},
  author={W Hsu and Ping-Lin Ong and Shih-Chun Chen and Long-Liu Lin},
  journal={Indian journal of biochemistry & biophysics},
  year={2009},
  volume={46 4},
  pages={281-8}
}
A serine residue Ser463, required for proper function of E. coli y-glutamyltranspeptidase (EcGGT) was identified by site-directed mutagenesis on the basis of sequence alignment of human, pig, rat, and three bacterial enzymes. Thr-, Asp-, and Lys-substituted variants were overexpressed in E. coli M15 cells and the recombinant proteins were purified to near homogeneity by nickel-chelate chromatography. With the exception of S463T, the other two variants completely lost GGT activity, implying the… CONTINUE READING