Final answer:
Noncompetitive inhibition of enzymes occurs when an inhibitor molecule binds to an allosteric site and blocks substrate binding to the active site, reducing the enzyme's activity.
Step-by-step explanation:
Noncompetitive inhibition of enzymes occurs when an inhibitor molecule binds to the enzyme in a location other than the active site, known as the allosteric site. This binding induces a conformational change in the enzyme that blocks substrate binding to the active site. As a result, the enzyme's activity is reduced.
Unlike competitive inhibition where the inhibitor competes with the substrate for the active site, noncompetitive inhibition does not require a structural similarity between the inhibitor and substrate. Thus, the addition of excess substrate does not reverse the inhibitory effect in noncompetitive inhibition.