Schellenberger W, Eschrich K, Hofmann E
Biomed Biochim Acta. 1983;42(1):57-72.
In a homogeneous and open enzyme system containing phosphofructokinase, pyruvate kinase, adenylate kinase, and glucose 6-phosphate isomerase the consequences of variations of the enzyme concentrations on the stationary enzyme activities have been investigated. An unexpected behavior was observed upon variation of the maximum activity of pyruvate kinase. Depending on the experimental conditions an increase of the concentration of pyruvate kinase resulted either in a diminution or in a stimulation of the stationary activity of this enzyme. An increase of the maximum activity of phosphofructokinase, however, stimulates both the activities of phosphofructokinase and pyruvate kinase. The experimental results are interpreted in terms of a mathematical model, based on the kinetic properties of the enzymes involved. The correlation between the observed changes of the activities of phosphofructokinase and pyruvate kinase and the appearance of multiple stationary states is discussed.
在一个含有磷酸果糖激酶、丙酮酸激酶、腺苷酸激酶和葡萄糖6-磷酸异构酶的均相开放酶系统中，研究了酶浓度变化对固定酶活性的影响。当丙酮酸激酶的最大活性发生变化时，观察到了一种意外的行为。根据实验条件，丙酮酸激酶浓度的增加要么导致该酶固定活性的降低，要么导致其受到刺激。然而，磷酸果糖激酶最大活性的增加会刺激磷酸果糖激酶和丙酮酸激酶的活性。根据基于所涉及酶的动力学性质的数学模型对实验结果进行了解释。讨论了观察到的磷酸果糖激酶和丙酮酸激酶活性变化与多个稳定状态出现之间的相关性。
