BIOMOLECULES AND ENZYMES

Detailed explanation-1: -In noncompetitive inhibition, the inhibitor binds at an allosteric site separate from the active site of substrate binding. Thus in noncompetitive inhibition, the inhibitor can bind its target enzyme regardless of the presence of a bound substrate.

Detailed explanation-2: -By decreasing the free-energy change of the reaction catalyzed by the enzyme. By binding to the substrate, thus changing its shape so that it no longer binds to the active site of the enzyme.

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: -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.