Agostinis P, Pinna L A, Meggio F, Marin O, Goris J, Vandenheede J R, Merlevede W
Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.
FEBS Lett. 1989 Dec 18;259(1):75-8. doi: 10.1016/0014-5793(89)81498-x.
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 beta-casein A(2), is readily phosphorylated by CK-1, but not by casein kinase-2(CK-2), cyclic AMP-dependent protein kinase, protein kinase C, phosphorylase kinase and protein kinase FA. Phosphorylation by CK-1 occurs only at Ser-6, Thr-8 being unaffected. The Km for the peptide is higher (1 mM) than for beta-casein A(2) (40 microM), while the Vmax 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.
源自β-酪蛋白A(2)中酪蛋白激酶-1（CK-1）磷酸化位点的合成肽Asp-Asp-Asp-Glu-Glu-Ser-Ile-Thr-Arg-Arg很容易被CK-1磷酸化，但不能被酪蛋白激酶-2（CK-2）、环磷酸腺苷依赖性蛋白激酶、蛋白激酶C、磷酸化酶激酶和蛋白激酶FA磷酸化。CK-1的磷酸化仅发生在Ser-6处，Thr-8不受影响。该肽的米氏常数（Km）（1 mM）高于β-酪蛋白A(2)（40 microM），而最大反应速度（Vmax）相当。这是迄今为止描述的首个用于CK-1的合成肽底物，可用于快速、特异性地估计粗提物中的CK-1活性。
