Enzyme kinetics at high enzyme concentration
Enzyme kinetics at high enzyme concentration
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DOI：
10.1006/bulm.1999.0163
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发表时间：
2000-05
影响因子：
3.5
通讯作者：
S. Schnell;P. Maini
中科院分区：
文献类型：
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作者：
S. Schnell;P. Maini
我们重新访问以前的经典Michaelis-Menten底物酶反应的分析，并在逆准稳态假设的帮助下，我们挑战近似d[C]/dt 0的基本酶反应在高酶浓度。首次报道了反应物浓度在时间上一致有效的近似解。数值模拟验证了这种解决方案。我们表明，可以找到一个解析近似的反应物，每个初始条件下使用适当的准稳态假设。本形式主义的一个优点是，它提供了一个新的程序拟合实验数据，以确定反应常数。最后，找到了一个新的必要判据，保证了反向准稳态假设的有效性。这在数字上得到了验证。
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with the aid of the reverse quasi-steady-state assumption, we challenge the approximation d[C]/dt ≈ 0 for the basic enzyme reaction at high enzyme concentration. For the first time, an approximate solution for the concentrations of the reactants uniformly valid in time is reported. Numerical simulations are presented to verify this solution. We show that an analytical approximation can be found for the reactants for each initial condition using the appropriate quasi-steady-state assumption. An advantage of the present formalism is that it provides a new procedure for fitting experimental data to determine reaction constants. Finally, a new necessary criterion is found that ensures the validity of the reverse quasi-steady-state assumption. This is verified numerically.