Inhibitors work by binding to the active site of an enzyme or a different site that affects the enzyme's activity. In competitive inhibition, the inhibitor competes with the substrate for the active site, effectively reducing the rate of the reaction. Non-competitive inhibitors bind to a different site, causing a conformational change in the enzyme, which decreases its activity regardless of substrate concentration. Uncompetitive inhibitors bind only to the enzyme-substrate complex, further decreasing activity. Allosteric inhibitors can bind to sites other than the active site, inducing changes that affect enzyme function.
