Eschrich K, Schellenberger W, Hofmann E
Biomed Biochim Acta. 1983;42(6):609-21.
The dynamic behaviour of an open futile cycle composed of phosphofructokinase and fructose 1,6-bisphosphatase has been investigated in a homogeneous reconstituted enzyme system in which the two enzymes cooperate with pyruvate kinase, adenylate kinase and glucose 6-phosphate isomerase. By the kinetic cooperation of phosphofructokinase and fructose 1,6-bisphosphatase various types of dynamic patterns can be generated. In the absence of fructose 1,6-bisphosphatase oscillations do not occur. As experimentally demonstrated, in a definite region of maximum activities of fructose 1,6-bisphosphatase sustained oscillations originate while at higher concentrations of the enzyme damped oscillations appear. At increasing concentrations of fructose 1,6-bisphosphatase damping is strengthened. Finally, at very high concentrations of fructose 1,6-bisphosphatase the metabolites relax monotonously to the stationary states. The observed oscillatory phenomena are mainly caused by the antagonistic effects of AMP on the kinetics of phosphofructokinase and fructose 1,6-bisphosphatase.
在一个均相重构酶系统中,对由磷酸果糖激酶和果糖1,6 -二磷酸酶组成的开放无效循环的动力学行为进行了研究,在该系统中这两种酶与丙酮酸激酶、腺苷酸激酶和葡萄糖6 -磷酸异构酶协同作用。通过磷酸果糖激酶和果糖1,6 -二磷酸酶的动力学协同作用,可以产生各种类型的动态模式。在没有果糖1,6 -二磷酸酶的情况下,不会发生振荡。如实验所示,在果糖1,6 -二磷酸酶最大活性的特定区域会产生持续振荡,而在该酶浓度较高时会出现阻尼振荡。随着果糖1,6 -二磷酸酶浓度的增加,阻尼增强。最后,在果糖1,6 -二磷酸酶浓度非常高时,代谢物会单调地弛豫到稳态。观察到的振荡现象主要是由AMP对磷酸果糖激酶和果糖1,6 -二磷酸酶动力学的拮抗作用引起的。