Voskoboev A I, Artsukevich I M, Ostrovskiĭ Iu M
Biokhimiia. 1978 Mar;43(3):460-6.
The kinetic analysis of bisubstrate enzymatic reaction catalysed by electrophoretically homogenous thiamine pyrophosphokinase (EC 2.7.6.2), isolated from rat liver has been carried out. Kinetic studies of the initial rates in the absence of the products and inhibition by the reaction products as well as the data from the equilibrium dialysis suggest that the reaction proceeds through the formation of a ternary enzyme-substrate complex. The combination with substrates and release of the products appears to be highly ordered. A possible scheme of the reaction mechanism is discussed.
对从大鼠肝脏中分离出的电泳纯硫胺素焦磷酸激酶（EC 2.7.6.2）催化的双底物酶促反应进行了动力学分析。在无产物情况下对初始速率的动力学研究、反应产物的抑制作用以及平衡透析数据表明，该反应通过形成三元酶 - 底物复合物进行。底物的结合和产物的释放似乎是高度有序的。讨论了反应机制的可能方案。
