Competitive inhibition occurs when a substance (inhibitor) binds directly to the active site of an enzyme, competing with the substrate for binding. Since both the substrate and inhibitor vie for the same site, the inhibitor prevents the enzyme from catalyzing the reaction unless more substrate is added to outcompete the inhibitor.
This type of inhibition increases the apparent Km (Michaelis constant) but does not change the Vmax because adding more substrate can eventually overcome the inhibition.
Why the Other Options Are Wrong:
Allosteric Inhibition
In this type of inhibition, the inhibitor binds at a site other than the active site (called the allosteric site).
This binding changes the enzyme’s shape, making it less effective or completely inactive.
Since the inhibitor does not compete for the active site, this is not competitive inhibition
Uncompetitive Inhibition
Here, the inhibitor binds only to the enzyme-substrate complex, not the free enzyme.
This type of inhibition lowers both Km and Vmax and cannot be reversed by increasing substrate concentration.
Since the inhibitor does not compete with the substrate for the active site, this is not competitive inhibition.
Irreversible Inhibition
In this type, the inhibitor binds permanently to the enzyme, often by forming covalent bonds.
This permanently deactivates the enzyme and cannot be overcome by adding more substrate.
Competitive inhibition, on the other hand, is reversible.
Non-Competitive Inhibition
Here, the inhibitor binds away from the active site and alters the enzyme’s shape.
It reduces the enzyme’s activity without being affected by substrate concentration.
Unlike competitive inhibition, increasing substrate concentration does not overcome non-competitive inhibition.