Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence.

@article{Ansai1996InteractionsBA,
  title={Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence.},
  author={Toshihiro Ansai and Lesley C Dupuy and S. Barik},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 40},
  pages={24401-7}
}
The protein phosphatase encoded by coliphage lambda (PPlambda) was found to be the equivalent of the minimal catalytic core of serine/threonine protein phosphatases (PP) by biochemical and mutational criteria. Bacterially expressed truncated versions of PP1 and PP5 phosphatases, representing the catalytic cores homologous to PPlambda, exhibited potent phosphatase activity. Unlike full-length PP1, but like PPlambda, the recombinant cores could use casein, p-nitrophenyl phosphate, and a wide… CONTINUE READING