Final answer:
Competitive inhibition involves inhibitors that bind to the enzyme's active site, competing with the substrate, which can be overcome by increasing substrate concentration. Non-competitive inhibition involves inhibitors that bind to an allosteric site, causing a conformational change that lowers the enzyme's maximal reaction rate irrespective of substrate concentration. Both are important for understanding drug mechanisms.
Step-by-step explanation:
Competitive inhibition occurs when an inhibitor molecule competes directly with the substrate by binding reversibly to the active site of an enzyme. This type of inhibition can be overcome at high substrate concentrations, as the substrate can outcompete the inhibitor for the enzyme binding, not affecting the maximal rate of the reaction.
Non-competitive inhibition, on the other hand, involves the binding of an inhibitor to an allosteric site on the enzyme. This binding induces a conformational change in the enzyme that affects its activity, thereby reducing the enzyme's affinity for the substrate and lowering the maximal rate of the reaction, regardless of how much substrate is present.
Understanding these mechanisms is crucial for developing therapeutic drugs, as many act by competitive or non-competitive inhibition to regulate enzyme activity.