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 K_m 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<K_m. The function is identical to the MM equation at [E]₀≦0.01K_m, while it is described as a new type of equation at 0.01K_m≦[E]₀<K_m. This function is of great significance in enzyme assays as a comprehensive approximation for the HMM-system.

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_米通过数值模拟。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_米。功能是相同的，在[对MM方程ë ] ₀ ≦0.01 ķ_米，而这是在0.01描述为新的类型的方程ķ_米≦[ ë ] ₀ < ķ_米。此功能作为HMM系统的全面近似，在酶分析中具有重要意义。