Question

How do allosteric enzymes activate and inhibit chemical reactions in a living organism?​

Answer 1

Answer:

Allosteric activators bind to locations on an enzyme away from the active site, inducing a conformational change that increases the affinity of the enzyme's active site(s) for its substrate(s). Allosteric inhibitors modify the enzyme's active site so that substrate binding is reduced or prevented.

Explanation:

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