BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The competitive inhibitor binds to the active site and prevents the substrate from binding there. The noncompetitive inhibitor binds to a different site on the enzyme; it doesn’t block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.

Detailed explanation-2: -The molecular basis for the binding of competitive inhibitors at the active site is that the substrate and the inhibitor are structurally similar, with the result that the enzyme is “deceived” into recognizing and binding the inhibitor.

Detailed explanation-3: -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-4: -A competitive inhibitor competes with the substrate for binding at the active site of the enzyme. A noncompetitive inhibitor binds at a site distinct from the active site.