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Relationship between enzyme concentration and Michaelis constant in enzyme assays.
Biochimie ( IF 3.3 ) Pub Date : 2020-06-23 , DOI: 10.1016/j.biochi.2020.06.002
Kyong-Il Yun 1 , Tong-Sul Han 1
Affiliation  

The upper bound of enzyme concentration for accurately estimating the parameters in Michaelis-Menten (MM) equation is not completely determined and still under discussion, even though many researchers have investigated the equation’s validity for a long time. In the paper, we broadly investigated the correlation between the system of ordinary differential equations for monosubstrate irreversible enzyme reaction (HMM-system) and its derivative MM equation focusing on the relationship between initial enzyme concentration [E]0 and Michaelis constant Km by numerical simulation. According to the results, the initial reaction velocity v0 is still a function of initial substrate concentration [S]0 at [E]0<Km. The function is identical to the MM equation at [E]0≦0.01Km, while it is described as a new type of equation at 0.01Km≦[E]0<Km. This function is of great significance in enzyme assays as a comprehensive approximation for the HMM-system.



中文翻译:

酶测定中酶浓度与米氏常数之间的关系。

尽管许多研究人员已长期研究该方程的有效性,但仍无法完全确定用于准确估计Michaelis-Menten(MM)方程参数的酶浓度上限。在论文中,我们广泛地研究了普通微分方程monosubstrate不可逆的酶反应(HMM系统)和它的衍生物MM方程集中于初始酶浓度之间的关系[的系统之间的相关性ë ] 0和米氏常数ķ通过数值模拟。根据结果​​,初始反应速度v 0仍是初始底物浓度的函数[ S] 0 在[ ë ] 0 < ķ。功能是相同的,在[对MM方程ë ] 0 ≦0.01 ķ,而这是在0.01描述为新的类型的方程ķ≦[ ë ] 0 < ķ。此功能作为HMM系统的全面近似,在酶分析中具有重要意义。

更新日期:2020-07-09
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