AP BIOLOGY

Detailed explanation-1: -Competitive inhibitors impair reaction progress by binding to an enzyme, often at the active site, and preventing the real substrate from binding. At any given time, only the competitive inhibitor or the substrate can be bound to the enzyme (not both). That is, the inhibitor and substrate compete for the enzyme.

Detailed explanation-2: -Competitive enzyme inhibitors possess a similar shape to that of the substrate molecule and compete with the substrate for the active site of the enzyme. This prevents the formation of enzyme-substrate complexes. Therefore, fewer substrate molecules can bind to the enzymes so the reaction rate is decreased.

Detailed explanation-3: -Final answer: In the presence of a competitive inhibitor, Vmax remains the same and KM increases.

Detailed explanation-4: -A competitive inhibitor competes with the substrate for the binding site on the enzyme. As substrate concentration increases, it eventually displaces the inhibitor. The reaction rate approaches the normal rate at higher substrate concentrations.