AP BIOLOGY

Detailed explanation-1: -The binding of this allosteric inhibitor changes the conformation of the enzyme and its active site, so the substrate is not able to bind. This prevents the enzyme from lowering the activation energy of the reaction, and the reaction rate is reduced.

Detailed explanation-2: -Inhibitor that resembles the enzyme’s normal substrate and competes for the active site. Reduces an enzyme’s productivity by blocking substrates from entering the active site.

Detailed explanation-3: -Competitive inhibitors work by camouflaging themselves as an enzyme’s natural substrate and binding to the enzyme’s active site, thereby blocking the natural substrate’s ability to bind to the enzyme’s active site. As binding affinity of a competitive inhibitor increases, enzyme activity decreases.

Detailed explanation-4: -Competitive inhibitors bind to the active sites of an enzyme and decrease the amount of binding of the substrate or ligand to enzyme. The result is that the Km is increased and Vmax remains the same. Ultimately, the chemical reaction can be reversed by increasing concentration of substrate.

Detailed explanation-5: -Explanation: Competitive inhibition involves the substrate’s access to the active site. In the case of competitive inhibition, the inhibitor blocks the substrate from the active site.