Questions: Which statement is false for a competitive inhibitor?
It is irreversible.
α′=1.
It is often structurally similar to the substrate.
It does not change Vmax.
Transcript text: Which statement is false for a competitive inhibitor?
It is irreversible.
$\alpha^{\prime}=1$.
It is often structurally similar to the substrate.
It does not change $V_{\text {max }}$.
Solution
Solution Steps
Step 1: Understanding Competitive Inhibition
Competitive inhibitors are molecules that bind to the active site of an enzyme, preventing the substrate from binding. This type of inhibition is characterized by the fact that it can be overcome by increasing the concentration of the substrate.
Step 2: Analyzing Each Statement
It is irreversible.
Competitive inhibition is typically reversible. The inhibitor can be displaced by increasing the concentration of the substrate.
\(\alpha^{\prime}=1\).
In competitive inhibition, \(\alpha^{\prime}\) is indeed equal to 1. This is because competitive inhibitors do not affect the enzyme-substrate complex once it is formed.
It is often structurally similar to the substrate.
Competitive inhibitors often resemble the substrate structurally, allowing them to bind to the active site of the enzyme.
It does not change \(V_{\text{max}}\).
Competitive inhibitors do not change the maximum velocity (\(V_{\text{max}}\)) of the enzyme-catalyzed reaction because the inhibition can be overcome by a high concentration of substrate.
Step 3: Identifying the False Statement
The statement "It is irreversible" is false for a competitive inhibitor, as competitive inhibition is typically reversible.