The influence of basic residues on the substrate specificity of protein kinase C.

@article{House1987TheIO,
  title={The influence of basic residues on the substrate specificity of protein kinase C.},
  author={Colin House and Richard E. H. Wettenhall and Bruce E. Kemp},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 2},
  pages={772-7}
}
The substrate specificity of protein kinase C has been examined using a series of synthetic peptide analogs of glycogen synthase, ribosomal protein S6, and the epidermal growth factor receptor. The glycogen synthase analog peptide Pro1-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala10 was phosphorylated at Ser7 with a Km of 40.3 microM. Peptide phosphorylation was strongly dependent on Arg4. When lysine was substituted for Arg4 the Km was increased approximately 20-fold. Addition of basic residues on… CONTINUE READING