Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40.
Glycogen synthase from rabbit skeletal muscle was found to be phosphorylated by a protein-tyrosine kinase, p40, purified from bovine thymus. The phosphorylation, to a stoichiometry of 0.4-0.5 mol/mol subunit, was specific for a single tyrosine residue in the sequence EEDGERYDEDEE. This acidic sequence has considerable similarity to the site recognized by p40 in erythrocyte band 3 protein. In the analysis of the phosphorylated peptide, it was noted that the sequence -RY(P)- impeded cleavage by either trypsin or automatic Edman degradation.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006006:Glycogen Synthase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000302:isolation & purification; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D011817:Rabbits; D013950:Thymus Gland / Q000201:enzymology*
D010748:Phosphopeptides; D006006:Glycogen Synthase; D011505:Protein-Tyrosine Kinases