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: -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.

Detailed explanation-3: -Competitive inhibitors bind to the active site of the enzyme and prevent substrates from binding to enzyme. This prevents the enzyme-substrate reaction from happening, thereby decreasing the activity of enzymes; however, competitive inhibitors can be overcome by increasing the concentration of substrates.

Detailed explanation-4: -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-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.