Kaĭmachnikov N P, Sel'kov E E
Biofizika. 1977 Mar-Apr;22(2):241-6.
A simple kinetic model was constructed to study the adaptation of cell energy metabolism to a varying loading. In this model the initiatory step of energy metabolism, in which the initial substrate S is activated at the expense of ATP molecule energy, is catalyzed by an oligomeric enzyme E dissociable at high ATP concentration to monomers E1. It is assumed that the steady state level of monomers E1 in the cell is maintained by constitutive synthesis of E1 molecules, which balances their continuous hydrolysis by proteases. The properties of the kinetic model were studied using a mathematical model which is a system of nonlinear differential equations describing the change with time of the total enzyme E concentration and the concentration of ATP. The main isoclines of this system can intersect in one, two or three points. The mathematical analysis shows that the kinetic model considered exhibits adaptive properties. A sharp increase of the ATPase activity in the model initiates a transient process which leads to a rise in the total enzyme E concentration and in the efficiency of energy metabolism. As a result, the concentration of ATP drops only slightly. The establishment of a new level of the enzyme E concentration may proceed in the oscillatory fashion.
构建了一个简单的动力学模型来研究细胞能量代谢对变化负荷的适应性。在该模型中,能量代谢的起始步骤,即初始底物S以ATP分子能量为代价被激活,由一种寡聚酶E催化,该酶在高ATP浓度下可解离为单体E1。假设细胞中单体E1的稳态水平通过E1分子的组成型合成来维持,这平衡了它们被蛋白酶持续水解的过程。使用一个数学模型研究了动力学模型的性质,该数学模型是一个非线性微分方程组,描述了总酶E浓度和ATP浓度随时间的变化。该系统的主要等斜线可以在一个、两个或三个点相交。数学分析表明,所考虑的动力学模型具有适应性。模型中ATP酶活性的急剧增加引发一个瞬态过程,导致总酶E浓度和能量代谢效率升高。结果,ATP浓度仅略有下降。酶E浓度新水平的建立可能以振荡方式进行。