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Opposite and mutually incompatible structural requirements of type‐2 casein kinase and cAMP‐dependent protein kinase as visualized with synthetic peptide substrates
Author(s) -
Pinna Lorenzo A.,
Meggio Flavio,
Marchiori Ferdinando,
Borin Gianfranco
Publication year - 1984
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(84)80490-1
Subject(s) - biochemistry , peptide , protein kinase a , kinase , residue (chemistry) , chemistry , phosphorylation , casein kinase 2 , casein , enzyme , casein kinase 2, alpha 1 , casein kinase 1 , protein kinase c , acetylation , mitogen activated protein kinase kinase , stereochemistry , gene
The synthetic hexapeptide Ser‐Glu‐Glu‐Glu‐Val‐Glu and its N‐acetylated derivative are readily and specifically phosphorylated by rat liver casein kinase TS (type‐2), while the derived heptapeptide with an additional N‐terminal Arg is a very poor substrate. Conversely, the substitution of Glu for Val 5 in the synthetic peptide Arg‐Arg‐Ser‐Thr‐Val‐Ala, which is a good substrate for cAMP‐dependent protein kinase by virtue of the N‐terminal arginyl residues, prevents its phosphorylation by this enzyme. These data indicate that the site specificities of these two classes of protein kinases, requiring acidic and basic residues on the C‐and N‐terminal sides of the target residue(s), respectively, are mutually incompatible.