Dadssi M, Duclos B, Cozzone A J
Laboratoire de Biologie Moléculaire, Centre National de la Recherche Scientifique, Villeurbanne, France.
Biochem Biophys Res Commun. 1989 Apr 28;160(2):552-8. doi: 10.1016/0006-291x(89)92468-6.
The phosphorylation in vitro of a series of exogenous peptides by E. coli protein kinases was studied. One of the substrates assayed, the hexapeptide Arg-Gly-Tyr-Ser-Leu-Gly, was found to be significantly phosphorylated at its serine residue. This finding provides the first example of an exogenous substrate utilizable by bacterial protein kinases. The kinetic parameters of the corresponding reaction were determined and the effect of various cations were analyzed. Magnesium, cobalt, manganese and zinc ions were all found to be activators, although to a varying extent. The results were discussed in terms of substrate specificity of bacterial protein kinases.
研究了大肠杆菌蛋白激酶对一系列外源肽的体外磷酸化作用。所检测的底物之一，六肽精氨酸-甘氨酸-酪氨酸-丝氨酸-亮氨酸-甘氨酸，被发现在其丝氨酸残基处发生了显著的磷酸化。这一发现提供了细菌蛋白激酶可利用的外源底物的首个实例。测定了相应反应的动力学参数，并分析了各种阳离子的作用。发现镁离子、钴离子、锰离子和锌离子均为激活剂，尽管激活程度不同。根据细菌蛋白激酶的底物特异性对结果进行了讨论。
