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A synthetic peptide containing the autophosphorylation site of the transforming protein of Harvey sarcoma virus is phosphorylated by the EGF‐stimulated tyrosine kinase
Author(s) -
Baldwin G.S.,
Stanley I.J.,
Nice E.C.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80619-x
Subject(s) - autophosphorylation , phosphorylation , tyrosine , epidermal growth factor , tyrosine kinase , threonine , biochemistry , tyrosine phosphorylation , biology , microbiology and biotechnology , kinase , peptide , chemistry , protein kinase a , signal transduction , serine , receptor
The transforming proteins (p21) of Harvey and Kirsten sarcoma viruses threonine kinase activity, which phosphorylates threonine 59 of the p21 proteins themselves. A tridecapeptide: Arg—Arg—Leu 56 —Asp—Thr—Thr 59 —Gly—Gln—Glu—Tyr—Ser—Ala 66 containing residues 56‐66 of p21 is phosphorylated solely on tyrosine by the epidermal growth factor (EGF)‐stimulated tyrosine kinase of A431 cell membranes. K m ‐Values of 240 and 80 μM and V max values of 1.7 and 0.1 nmol.min −1 .mg −1 were obtained in the presence and absence of EGF, respectively.