BIOMOLECULES AND ENZYMES

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

Detailed explanation-3: -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.

Detailed explanation-4: -In the case of competitive inhibition, the effect of the inhibitor could be reduced and eventually overwhelmed with increasing amounts of substrate. This was because increasing substrate made increasing percentages of the enzyme active.