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Partially dephosphorylated phosphopeptide AcSer(P)‐Ser(P)‐Ser(P) is an excellent substrate for casein kinase‐2
Author(s) -
Meggio Flavio,
Perich John W.,
Johns Reginald B.,
Pinna Lorenzo A.
Publication year - 1988
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(88)80206-0
Subject(s) - phosphopeptide , phosphoserine , dephosphorylation , phosphorylation , chemistry , substrate (aquarium) , biochemistry , kinase , peptide , phosphatase , casein , cleavage (geology) , casein kinase 1 , protein kinase a , serine , biology , ecology , paleontology , fracture (geology)
The synthetic phosphopeptide AcSer(P)‐Ser(P)‐Ser(P), reproducing a recurrent feature of casein and other phosphoproteins, once partially dephosphorylated by acid phosphatase, serves as an efficient substrate for casein kinase‐2. Previous dephosphorylation beyond 30% hinders subsequent phosphorylation and the entirely dephosphorylated peptide is not a substrate at all. The kinetic constants of the partially dephosphorylated phosphopeptide are much more favourable than those of the synthetic peptides SEEEAA, SSEE and SEE, the latter one being totally inert. Optimal phosphorylation occurs at pH values that ensure complete ionization of the phosphoseryl side chains. These data provide incontrovertible demonstration that phosphoserine can replace carboxylic amino acids as specificity determinant for CK‐2, being more effective than glutamic acid itself.