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A synthetic peptide substrate specific for casein kinase‐1
Author(s) -
Agostinis Patrizia,
Pinna Lorenzo A.,
Meggio Flavio,
Marin Oriano,
Goris Jozef,
Vandenheede Jackie R.,
Merlevede Wilfried
Publication year - 1989
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(89)81498-x
Subject(s) - peptide , casein , substrate (aquarium) , chemistry , substrate specificity , casein kinase 1 , biochemistry , protein kinase a , kinase , biology , enzyme , ecology
The synthetic peptide, Asp‐Asp‐Asp‐Glu‐Glu‐Ser‐Ile‐Thr‐Arg‐Arg, derived from the phosphorylation site of casein kinase‐1 (CK‐1) in β‐casein A 2 , is readily phosphorylated by CK‐1, but not by casein kinase‐2 (CK‐2), cyclic AMP‐dependent protein kinase, protein kinsae C, phosphorylase kinase and protein kinase F a . Phosphorylation by CK‐1 occurs only at Ser‐6, Thr‐8 being unaffected. The K m for the peptide is higher (1 mM) than for β‐casein A 2 (40 μM), while the V max is quite comparable. This is the first synthetic peptide substrate for CK‐1 described so far, and can be used for the rapid and specific estimation of CK‐1 activity in crude extracts.