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: -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: -Which of the following statements is true about competitive inhibitors? Explanation: Competitive inhibition is a common type of reversible inhibition. The apparent Km increases in the presence of inhibitor by a factor . The maximum velocity for the reaction remains same in the presence of a competitive inhibitor.