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: -Noncompetitive inhibition, a type of allosteric regulation, is a specific type of enzyme inhibition characterized by an inhibitor binding to an allosteric site resulting in decreased efficacy of the enzyme. An allosteric site is simply a site that differs from the active site-where the substrate binds.

Detailed explanation-3: -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-4: -The allosteric inhibitor binds to an enzyme at a site other than the active site. The shape of the active site is altered so that the enzyme can no longer bind to its substrate.

Detailed explanation-5: -The allosteric site is the site, which is not the active site, where some drugs bind to an enzyme. Due to this, the shape of the enzyme changes, it becomes difficult for the substrate to recognize the active site of the enzyme. This represents non-competitive inhibition.