I only recently learned about the Michaelis-Menten equation, since I am not studying biology or anything related. Let's write the equation as $$\frac{d[P]}{dt} = V_{max} \cdot \frac{[S]}{K + [S]}$$ If I'm not mistaken, this equation describes the rate at which products are formed ($\frac{d[P]}{dt}$) as a function of substrate concentration $[S]$ in steady-state. In a translation of Michaelis' paper I read that $V_{max}$ can be written as $k [E]$, where $k$ is a constant and $[E]$ is the total enzyme concentration.
Mathematically one would say that when the total enzyme concentration is zero ($[E] = 0$), the rate at which the product is formed should equal zero. If I recall correctly, in several reactions products are formed without enzymes (Enzymes only enhance the reaction rate?). Is the Michaelis-Menten equation specifically used for situations where $[E]>0$? If so, how does it account for very low enzyme concentrations where product formation from non-enzyme reactions cannot be neglected?