Final answer:
Irreversible inhibitors form covalent bonds with amino acids in the active site of an enzyme, permanently inactivating it.
Step-by-step explanation:
An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. This type of inhibitor forms a strong, permanent bond with an amino acid in the active site, preventing the substrate from binding to the enzyme and stopping catalysis from occurring. For example, some irreversible inhibitors, like penicillin, covalently bind to enzymes needed for cell wall formation in bacteria, permanently inactivating them. These inhibitors cannot be easily dissociated, making their inhibition irreversible.