Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl.
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.
Wu
J J
JJ
Selectide Corporation, A Subsidiary of Hoechst Marion Roussel, Inc., Tucson, AZ 85737, USA.
Phan
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Lam
K S
KS
D000595:Amino Acid Sequence; D016044:Fusion Proteins, bcr-abl / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D019151:Peptide Library; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D016315:Proto-Oncogene Proteins c-abl / Q000378:metabolism*; D013379:Substrate Specificity
D009842:Oligopeptides; D019151:Peptide Library; D011505:Protein-Tyrosine Kinases; D016044:Fusion Proteins, bcr-abl; D016315:Proto-Oncogene Proteins c-abl