BIOCHEMISTRY
ENZYMES AND METABOLISM
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding
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Binds to the active site and blocks it from binding substrate
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Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate
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Binds directly to the active site and mimics the substrate
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Detailed explanation-1: -An allosteric inhibitor binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate. Hence option c is the correct answer.
Detailed explanation-2: -Allosteric inhibitors modify the active site of the enzyme so that substrate binding is reduced or prevented. In contrast, allosteric activators modify the active site of the enzyme so that the affinity for the substrate increases.
Detailed explanation-3: -The allosteric inhibitor lowers the temperature of the active site. The allosteric inhibitor binds to the substrate and prevents it from binding at the active site. The allosteric inhibitor causes a structural change in the enzyme that prevents the substrate from binding at the active site.
Detailed explanation-4: -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).
Detailed explanation-5: -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.