Influence of acidic residues on substrate specificity of oncogene products pp60v-src and p56lck in vitro.
Substrate specificities of two protein tyrosine kinases were compared using nine undecapeptides modeled after human gastrin. Using the proto-oncogene product, p56lck, Vmax decreased with the distance between glutamate and tyrosine, whereas for the oncogene product, pp60v-src there was no relation. For pp60v-src there was a precipitous rise in Km, from 2.9 to 20 mM when glutamate was greater than three residues away from tyrosine. For p56lck, Km was a minimum when glutamate occupied either a position 3 residues, or both positions 3 and 4, N-terminal to tyrosine. An important factor in enzyme recognition of these peptides is glutamate three residues N-terminal to tyrosine.
Tinker
D A
DA
University of Texas M.D. Anderson Cancer Center, Houston 77030.
Cartron
J L
JL
McMurray
J S
JS
Levin
V A
VA
D000595:Amino Acid Sequence; D000818:Animals; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D051379:Mice; D008969:Molecular Sequence Data; D015688:Oncogene Protein pp60(v-src) / Q000737:chemistry*; D011487:Protein Conformation; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins; D011505:Protein-Tyrosine Kinases; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D015688:Oncogene Protein pp60(v-src)