Sauro H M, Kacser H
Department of Genetics, University of Edinburgh, Scotland.
Eur J Biochem. 1990 Feb 14;187(3):493-500. doi: 10.1111/j.1432-1033.1990.tb15330.x.
The association of different enzymes into a complex may induce changes in the kinetic parameters of its component enzymes. This implies that they cannot be treated as independent catalysts. It will affect the formulations and theorems of control analysis and necessitates the introduction of additional elasticities reflecting the effect of one enzyme on the rate of another. We show how this is achieved as an extension of the classical treatment. We present modified summation and connectivity theorems incorporating both homologous and heterologous interactions. The case of channelling of metabolites in such complexes is considered and an experimental method for its detection is suggested.
不同的酶结合形成复合物可能会导致其组成酶的动力学参数发生变化。这意味着它们不能被视为独立的催化剂。这将影响控制分析的公式和定理,因此需要引入额外的弹性系数来反映一种酶对另一种酶反应速率的影响。我们展示了如何通过扩展经典处理方法来实现这一点。我们提出了包含同源和异源相互作用的修正求和定理和连通性定理。我们考虑了代谢物在这种复合物中的通道化情况,并提出了一种检测它的实验方法。