Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl

Jinzi J. Wu, Hoang Phan, Kit Lam

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

We studied the intrinsic tyrosine kinase activity and substrate specificity of c-Abl and Bcr-Abl protein tyrosine kinases (PTKs) using the peptide substrates discovered from a synthetic combinatorial peptide library. Our data indicate that the phosphorylation of these peptides by Bcr-Abl was consistently stronger than that by c-Abl. Bcr-Abl also showed substrate preference towards those peptides with one or more positive charges.

Original languageEnglish (US)
Pages (from-to)2279-2284
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume8
Issue number17
DOIs
StatePublished - Sep 8 1998
Externally publishedYes

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Substrate Specificity
Phosphotransferases
Protein-Tyrosine Kinases
Peptides
Substrates
bcr-abl Fusion Proteins
Peptide Library
Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl. / Wu, Jinzi J.; Phan, Hoang; Lam, Kit.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 8, No. 17, 08.09.1998, p. 2279-2284.

Research output: Contribution to journalArticle

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