Explain how allosteric regulation can influence the activity of an enzyme's active site.
Instructor solution
Allosteric regulation involves the binding of regulatory molecules to sites other than the active site, known as allosteric sites. This binding can induce conformational changes in the enzyme that either enhance or inhibit its activity. When an allosteric activator binds, it can increase the enzyme's affinity for the substrate, enhancing its activity. Conversely, an allosteric inhibitor can decrease the enzyme's affinity for the substrate, reducing its activity.
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What is the effect of an allosteric inhibitor on an enzyme?
- A.
It increases the enzyme's affinity for the substrate.
- B.
It permanently deactivates the enzyme.
- C.
It decreases the enzyme's affinity for the substrate.
- D.
It has no effect on the enzyme's activity.
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