Faculty Collaboration Database

Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides. Biochem Biophys Res Commun 1990 Mar 30;167(3):1333-40

Date

03/30/1990

Pubmed ID

2157430

DOI

10.1016/0006-291x(90)90669-e

Scopus ID

2-s2.0-0025322269 (requires institutional sign-in at Scopus site)   4 Citations

Abstract

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.

Author List

Rönnstrand L, Sorokin A, Engström U, Heldin CH

Author

Andrey Sorokin PhD Professor in the Medicine department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Humans
Kinetics
Molecular Sequence Data
Oligopeptides
Phosphorylation
Platelet-Derived Growth Factor
Protein Kinases
Receptors, Cell Surface
Receptors, Platelet-Derived Growth Factor
Recombinant Proteins
Substrate Specificity