Final answer:
An irreversible inhibitor permanently inactivates an enzyme by forming a covalent bond at the active site, leading to permanent inhibition which cannot be reversed.
Step-by-step explanation:
The kind of inhibitor that binds very tightly to an enzyme, often forming a covalent bond with an amino acid in the active site, is an irreversible inhibitor. This type of inhibitor inactivates the enzyme by bonding covalently to a specific group within the active site. Such irreversible binding results in permanent inhibition of the enzyme activity because the enzyme-inhibitor bond cannot be dissociated; hence, this process cannot be reversed.