Unique biochemical properties of the protein tyrosine phosphatase activity of PTEN-demonstration of different active site structural requirements for phosphopeptide and phospholipid phosphatase activities of PTEN.

@article{Chia2010UniqueBP,
  title={Unique biochemical properties of the protein tyrosine phosphatase activity of PTEN-demonstration of different active site structural requirements for phosphopeptide and phospholipid phosphatase activities of PTEN.},
  author={Joel Yeong-Chit Chia and Joanna E Gajewski and Yi Xiao and Hong-Jian Zhu and Heung-Chin Cheng},
  journal={Biochimica et biophysica acta},
  year={2010},
  volume={1804 9},
  pages={1785-95}
}
Missense PTEN mutations of the active site residues Asp-92, Cys-124 and Gly-129 contribute to Cowden syndrome. How their mutations affect phospholipid phosphatase activity and tumor suppressor function of PTEN has been defined. In this study, we investigated how their mutations affect the kinetics and catalytic mechanism of PTEN phosphoprotein phosphatase activity. Our data suggest that PTEN catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys-124 transiently… CONTINUE READING