The active site substrate specificity of the cAMP-dependent protein kinase

Y. G. Kwon, M. Mendelow, J. Srinivasan, Ryong Lee Tae Ryong Lee, S. Pluskey, A. Salerno, D. S. Lawrence

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


cAMP-dependent protein kinase substrates have been synthesized employing an unusually efficient method that allows the alcohol-bearing residue to be incorporated into the peptide after solid phase peptide synthesis. These peptide substrates have been utilized to map the active site substrate specificity of the protein kinase. Only α- or β-substituted alcohol- bearing residues containing the proper absolute configuration are phosphorylated by the enzyme. However, the cAMP-dependent protein kinase will phosphorylate achiral residues. The implications of the observed protein kinase substrate specificity with respect to inhibitor design are discussed.

Original languageEnglish
Pages (from-to)10713-10716
Number of pages4
JournalJournal of Biological Chemistry
Issue number15
Publication statusPublished - 1993

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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