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

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

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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
Issue number3
Publication statusPublished - 1995

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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