AP BIOLOGY

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: -In non-competitive inhibition, the inhibitor binds to an allosteric site and prevents the enzyme-substrate complex from performing a chemical reaction. This does not affect the Km (affinity) of the enzyme (for the substrate).

Detailed explanation-3: -The allosteric activator binds to an enzyme at a site other than the active site. The shape of the active site is changed, allowing substrate to bind at a higher affinity. Pretty much all cases of noncompetitive inhibition (along with some unique cases of competitive inhibition) are forms of allosteric regulation.

Detailed explanation-4: -Noncompetitive inhibitors bind to allosteric sites on the enzyme and prevent the substrate-enzyme interaction by altering the active site.

Detailed explanation-5: -In noncompetitive inhibition (also known as allosteric inhibition), an inhibitor binds to an allosteric site; the substrate can still bind to the enzyme, but the enzyme is no longer in optimal position to catalyze the reaction.