How does mechanism-based inhibition differ from other forms of enzyme inhibition?

Mechanism-based inhibition is characterized by its ability to irreversibly alter the active site of an enzyme, significantly affecting its functionality. This type of inhibition often involves the inhibitor being processed by the enzyme as if it were a substrate, leading to the formation of a reactive intermediate that covalently binds to the enzyme's active site. This covalent modification prevents the enzyme from catalyzing its normal reaction, effectively inactivating it.

Unlike competitive inhibition, where the inhibitor competes with substrates for the active site but does not permanently affect the enzyme, mechanism-based inhibition results in a permanent change to the enzyme's structure. It is also not limited to high temperatures or dependent on the presence of specific cofactors, which differentiates it from other forms of enzyme inhibition that may rely on these conditions. Instead, the defining feature of mechanism-based inhibition is its irreversible alteration of the enzyme, leading to long-lasting effects on its activity.