Which of the following statements are true regarding a competitive inhibitor? Select all that apply

Competitive inhibition occurs when a molecule similar in structure to the substrate competes for the same binding site on an enzyme. This prevents the formation of the enzyme-substrate complex, thereby reducing the rate of reaction. In Michaelis-Menten kinetics, competitive inhibitors increase the Km (Michaelis constant) because a higher concentration of substrate is needed to reach half-maximal velocity, while the Vmax remains unchanged. Rationale: A. This statement is incorrect because the inhibitor and the substrate cannot bind to the active site at the same time. The binding is mutually exclusive; if the inhibitor occupies the site, the substrate is blocked. Competitive inhibition is defined by this binary competition for a single molecular coordinates on the enzyme surface. B. Inhibition can be overcome by high [S] is a hallmark of competitive inhibition. As the substrate concentration increases, the probability of a substrate molecule outcompeting an inhibitor molecule for the active site increases. At sufficiently high concentrations, the enzyme can still reach its maximum velocity (Vmax), effectively masking the presence of the inhibitor. C. Inhibitor binds to active site of the enzyme is true and describes the fundamental mechanism of this process. The inhibitor often mimics the transition state or the molecular structure of the substrate to fit into the catalytic pocket. This direct occupation of the active site is what distinguishes it from allosteric or non-competitive inhibition. D. This statement describes non-competitive or allosteric inhibition, where the inhibitor binds to a regulatory site different from the active site. In such cases, increasing substrate concentration does not reverse the inhibition. In competitive inhibition, the substrate and inhibitor must target the exact same site on the enzyme molecule. E. An inhibitor is generally not a substrate and is not broken down by the enzyme. The purpose of an inhibitor is to occupy the site and remain there to prevent catalytic activity. If the enzyme could break down the inhibitor, the molecule would simply be a competing substrate, not a true clinical or biochemical inhibitor.