Venieratos D, Goldbeter A
Biochimie. 1979;61(11-12):1247-56. doi: 10.1016/s0300-9084(80)80284-7.
The study of a concerted allosteric model for an enzyme activated by the reaction product shows that this system can generate sustained metabolic oscillations regardless of the number of protomers constituting the enzyme. The analysis extends the results previously obtained in a dimeric model for the phosphofructokinase reaction which produces glycolytic periodicities. When the substrate and product concentrations evolve on comparable time scales, the amplitude of oscillations significantly drops as the number of enzyme subunits evolves from 2 to 8. The width of the domain of substrate injection rates which produce oscillations and the periodic variation in enzyme activity also depend on the number of protomers and on the time scale structure of the system. Theoretical predictions are compared with the experiments on glycolytic oscillations in yeast and muscle, and with the structural characteristics of phosphofructokinase. The results are also discussed in relation with the mechanism of cyclic AMP oscillations in the slime mold Dictyostelium discoideum.
对由反应产物激活的酶的协同变构模型的研究表明，无论构成该酶的原体数量如何，此系统都能产生持续的代谢振荡。该分析扩展了先前在产生糖酵解周期性的磷酸果糖激酶反应的二聚体模型中所获得的结果。当底物和产物浓度在相当的时间尺度上演变时，随着酶亚基数量从2增加到8，振荡幅度会显著下降。产生振荡的底物注入速率域的宽度以及酶活性的周期性变化也取决于原体数量和系统的时间尺度结构。理论预测与酵母和肌肉中糖酵解振荡的实验以及磷酸果糖激酶的结构特征进行了比较。还结合盘基网柄菌中环状AMP振荡的机制对结果进行了讨论。
