Malkova I A, Popova S V, Sel'kov E E
Biofizika. 1980 May-Jun;25(3):503-7.
A quantitative mathematical model of two-substrate reaction catalized by phosphofructokinase from E. coli has been investigated. The model takes into account the tetrameric enzyme structure and resulting kinetic peculiarities of the reaction catalized, in particular, iso-and alosteric effects of ADP on enzyme activity. Fitting of the model parameters to experimental data allowed to approximate these data with good accuracy. The ranges of admitted rates of fructose-6-phosphate input and ATP regeneration at which autooscillations and multiple steady-states occur in the system have been calculated. A minimal open system with three enzymes has been proposed for experimental demonstration of the autooscillatory behaviour.
对大肠杆菌磷酸果糖激酶催化的双底物反应的定量数学模型进行了研究。该模型考虑了四聚体酶结构以及由此产生的催化反应的动力学特性，特别是ADP对酶活性的同工和变构效应。将模型参数与实验数据拟合后，能够以较高的精度对这些数据进行近似。计算了系统中发生自振荡和多重稳态时6-磷酸果糖输入和ATP再生的允许速率范围。为了对自振荡行为进行实验验证，提出了一个具有三种酶的最小开放系统。
