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: -A competitive inhibitor competes with substrate for binding to an active site. When the inhibitor occupies the active site, it forms an enzyme-inhibitor complex and the enzyme cannot react (Fig.

Detailed explanation-3: -In noncompetitive allosteric inhibition, inhibitor molecules bind to an enzyme at the allosteric site. Their binding induces a conformational change that reduces the affinity of the enzyme’s active site for its substrate.

Detailed explanation-4: -Noncompetitive inhibition of an enzyme can occur when an inhibitor binds to an enzyme at a site other than the active site. The noncompetitive inhibitor slows down the reaction rate, i.e. the rate of the product formation is less with inhibitor present than with inhibitor absent.

Detailed explanation-5: -This type of inhibition decreases the turnover rate of an enzyme rather than interfering with the amount of substrate binding to the enzyme. The reaction is slowed rather than stopped. Non-competitive inhibition, therefore, cannot be increased by increasing the substrate.