Final answer:
Competitive inhibitors bind to the active site of enzymes, while noncompetitive inhibitors bind to allosteric sites outside the active site. Competitive inhibitors compete with the substrate for binding, while noncompetitive inhibitors change the enzyme's conformation. Competitive inhibition can be overcome by increasing substrate concentration, but noncompetitive inhibition cannot.
Step-by-step explanation:
Competitive inhibitors bind to the active site of an enzyme, competing with the substrate for binding. These inhibitors structurally resemble the substrate and block the enzyme's activity. Increasing the concentration of the substrate can overcome the inhibition by outnumbering the inhibitor. Noncompetitive inhibitors, on the other hand, bind to an allosteric site outside the active site. They change the conformation of the enzyme, preventing the substrate from fitting into the active site properly. Noncompetitive inhibition is not affected by substrate concentration and cannot be overcome by increasing substrate concentration.