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In contrast, for a noncompetitive inhibitor, the plots for separate experiments at different inhibitor concentrations will intersect on the 1/[S] axis
When an inhibitor attaches to the enzyme at a location other than the active site, noncompetitive inhibition takes place. The allosteric site is the name given to this alternative location. The active site is changed as a result, and the substrate and enzyme are no longer tightly bound.
Because of this, the enzyme is unable to catalyze the reaction. Increases in substrate concentrations will have no effect on the inhibitor's effect because the substrate and inhibitor do not compete directly.
Biochemical catalysts called enzymes quicken chemical reactions. Due of their extreme specificity, enzymes can only regulate certain processes. By reducing the reaction's activation energy, these biological catalysts facilitate reactions. The power necessary for a reaction to occur is known as activation energy.
These reactions can be carried out more rapidly by reducing the activation energy. In order to avoid the need for energy-intensive random collisions, reactants are swiftly brought together by enzymes. The active site is where an enzyme binds to the reactants, also known as substrates, to form an enzyme-substrate complex. Once bound, the enzyme positions the reactants in a way that requires less energy for their molecules to interact. As a result, the product might form quickly. The enzyme is freed when the reaction is complete to work on another reaction.
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