Uncompetitive Inhibition: Kinetic Impact
| Parameter | Change in Uncompetitive Inhibition |
|---|---|
 Latex |
Decreases (The inhibitor binds only to the enzyme-substrate complex, effectively removing it from the reaction). |
| $Latex K_m $Latex | Decreases (Le Chatelier’s principle: tying up the $ES$ complex draws more enzyme into the complex, appearing to increase affinity). |
High-Yield Core Realities:
- Binding Mechanism: The inhibitor binds only to the enzyme-substrate ($ES$) complex, not the free enzyme ($E$).
- Lineweaver-Burk Plot: Uncompetitive inhibition results in parallel lines on the plot. Because both $V_{max}$ and $K_m$ decrease by the same proportion, the lines for the uninhibited and inhibited reactions have the same slope, but different x- and y-intercepts.
- Clinical Comparison: Unlike competitive inhibition, increasing the concentration of substrate $[S]$ cannot overcome uncompetitive inhibition.