The design of peptide-based substrates for the cdc2 protein kinase

J. Srinivasan, M. Koszelak, M. Mendelow, Y. G. Kwon, D. S. Lawrence

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Abstract

The substrate sequence specificity of the cdc2 protein kinase from Pisaster ochraceus has been evaluated. The peptide, Ac-Ser-Pro-Gly-Arg-Arg-Arg-Arg-Lys-amide, serves as an efficient cdc2 kinase substrate with a K(m) of 1.50 ± 0.04 μM and a V(max) of 12.00 ± 0.18 μmol/min per mg. The amino acid sequence of this peptide is not based on any sequence in a known protein substrate of the cyclin-dependent kinase, but rather was designed from structural attributes that appear to be important in the majority of cdc2 substrates. This cyclin-dependent enzyme is remarkably indiscriminate in its ability to recognize and phosphorylate peptides that contain an assortment of structurally diverse residues at the P-2, P-1 and P+2 positions. However, peptides that contain a free N-terminal serine or lack an arginine at the P+4 position are relatively poor substrates. These aspects of the substrate specificity of the cdc2 protein kinase are compared and contrasted with the previously reported substrate specificity of a cdc2-like protein kinase from bovine brain.

Original languageEnglish
Pages (from-to)927-931
Number of pages5
JournalBiochemical Journal
Volume309
Issue number3
DOIs
Publication statusPublished - 1995 Jan 1

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Srinivasan, J., Koszelak, M., Mendelow, M., Kwon, Y. G., & Lawrence, D. S. (1995). The design of peptide-based substrates for the cdc2 protein kinase. Biochemical Journal, 309(3), 927-931. https://doi.org/10.1042/bj3090927