Kochetkov S N, Khachatrian L L, Bagirov E M, Sashchenko L P, Severin E S
Biokhimiia. 1978 Jan;43(1):150-5.
Interaction of several nucleotide derivates with homogenous catalytic subunit of cyclo-AMP-dependent histone kinase from pig brain is studied. Inhibition constants of these compounds are calculated, and the affinity of inhibitors to the enzyme active site is evaluated. The nature of heterocyclic base is found to be the main contribution into binding with substrate. The enzyme specificity with respect to a number of bivalent metal ions is studied, and Mg2+ is demonstrated to be the only efficient enzyme activator. It is shown by means of stationary kinetics that histone kinase-catalysed phosphotransferase reaction has a "ping-pong"-like mechanism.
研究了几种核苷酸衍生物与猪脑环磷酸腺苷依赖性组蛋白激酶的同源催化亚基之间的相互作用。计算了这些化合物的抑制常数，并评估了抑制剂对酶活性位点的亲和力。发现杂环碱的性质是与底物结合的主要贡献因素。研究了该酶对多种二价金属离子的特异性，结果表明Mg2+是唯一有效的酶激活剂。通过稳态动力学表明，组蛋白激酶催化的磷酸转移酶反应具有类似“乒乓”的机制。
