Kuroda Y, Hashimoto E, Ku Y, Nishizuka Y
J Biochem. 1979 Apr;85(4):1099-101. doi: 10.1093/oxfordjournals.jbchem.a132418.
Cyclic AMP-dependent and cyclic GMP-dependent protein kinases (protein kinases A and G, respectively) utilize the same phosphate acceptor proteins when assayed in in vitro systems. Nevertheless, protein kinase A phosphorylates preferentially free histone, whereas protein kinase G greatly favors the histone which is associated with polydeoxyribonucleotide. On the other hand, when cytoplasmic soluble substrates such as phosphorylase kinase are used, the reactions are always more favorable for protein kinase A rather than for protein kinase G. Available evidence implies that the topographic relationship between enzyme and substrate may be an important determining factor for the functional specificities of these two classes of protein kinases.
环磷酸腺苷依赖性和环磷酸鸟苷依赖性蛋白激酶(分别为蛋白激酶A和蛋白激酶G)在体外系统中进行测定时,利用相同的磷酸受体蛋白。然而,蛋白激酶A优先磷酸化游离组蛋白,而蛋白激酶G则极大地倾向于与多脱氧核糖核苷酸结合的组蛋白。另一方面,当使用细胞质可溶性底物如磷酸化酶激酶时,反应总是对蛋白激酶A比对蛋白激酶G更有利。现有证据表明,酶与底物之间的拓扑关系可能是这两类蛋白激酶功能特异性的重要决定因素。