Pure noncompetitive inhibition

Set $K_i=K_i^{\prime }$, so that $\alpha ={\alpha }^{\prime }$. The reversible enzyme inhibition equation reduces toAt the chosen $I=30\mu \mathrm{M}$, every reaction rate is one quarter of its uninhibited value. The plateau falls to $25\mu \mathrm{M}\mathrm{mi}{\mathrm{n}}^{-1}$, but half that plateau still occurs at $s=20\mu \mathrm{M}$. Increasing substrate cannot restore the uninhibited plateau. An unchanged apparent Michaelis constant here expresses equality of the two binding effects, rather than an absence of inhibitor binding to the enzyme-substrate complex.