This document discusses irreversible inhibition, which is when an inhibitor forms a covalent bond with an enzyme, permanently inactivating it. There are three types of irreversible inhibitors: group specific reagents that react with amino acid side chains like serine; affinity labels that are substrate analogs that covalently bind the active site; and suicide inhibitors that are processed by the enzyme into a reactive intermediate that modifies the enzyme. Examples discussed include nerve agents that inhibit acetylcholinesterase, aspirin inhibiting cyclooxygenase, and allopurinol being oxidized by xanthine oxidase to form a stronger inhibitor. Irreversible inhibitors have clinical importance as some drugs work through this mechanism.