A transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stability

被引:4
|
作者
Mallory, Kristina [1 ]
Van Gorder, Robert A. [1 ]
机构
[1] Univ Cent Florida, Dept Math, Orlando, FL 32816 USA
关键词
Dynamic Michaelis-Menten model; Nonlinear dynamics; Stability; Enzyme reactions; KINETICS;
D O I
10.1007/s10910-013-0257-1
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The dynamic form of the Michaelis-Menten enzymatic reaction equations provide a time-dependent model in which a substrate reacts with an enzyme to form a complex which in turn is converted into a product and the enzyme . In the present paper, we show that this system of four nonlinear equations can be reduced to a single nonlinear differential equation, which is simpler to solve numerically than the system of four equations. Applying the Lyapunov stability theory, we prove that the non-zero equilibrium for this equation is globally asymptotically stable, and hence that the non-zero steady-state solution for the full Michaelis-Menten enzymatic reaction model is globally asymptotically stable for all values of the model parameters. As such, the steady-state solutions considered in the literature are stable. We finally discuss properties of the numerical solutions to the dynamic Michaelis-Menten enzymatic reaction model, and show that at small and large time scales the solutions may be approximated analytically.
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页码:222 / 230
页数:9
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