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Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides

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Author

Summary, in English

Synthetic peptides derived from the sequence surrounding tyrosine-857 in the human platelet-derived growth factor (PDGF) beta-receptor were used to elucidate the requirement for length and presence of negative and positively charged amino acids in substrates of the PDGF beta-receptor protein tyrosine kinase. The measured Km for the different peptides were all in the range 1-10 mM. A peptide of only five amino acids, lacking acidic amino acid residues, were found to be substrates for the receptor kinase. Ligand binding was found to stimulate the phosphorylation of peptides mainly by lowering the Km both for peptide and for ATP. Only minor changes in the Vmax occurred upon stimulation with PDGF. The reaction mechanism was found to be sequential, i.e. both the peptide and ATP have to bind to the enzyme before any product is released.

Publishing year

1990

Language

English

Pages

1333-1340

Publication/Series

Biochemical and Biophysical Research Communications

Volume

167

Issue

3

Document type

Journal article

Publisher

Elsevier

Topic

  • Medicinal Chemistry

Keywords

  • Platelet-Derived Growth Factor Recombinant Proteins/metabolism Substrate Specificity
  • Cell Surface/*metabolism Receptors
  • Amino Acid Sequence Humans Kinetics Molecular Sequence Data Oligopeptides/chemical synthesis/*metabolism/pharmacology Phosphorylation Platelet-Derived Growth Factor/metabolism Protein Kinases/*metabolism Receptors

Status

Published

ISBN/ISSN/Other

  • ISSN: 1090-2104