Which of the following strategies of enzymatic inhibition is used by noncompetitive inhibitors?
Correct answer: D. Bind to an allosteric site to cause a conformational shift in the enzyme
- A. Bind to substrate so that it cannot bind to the active site
- B. Target the enzyme for destruction using a protease
- C. Bind to the active site and prevent substrate from binding
- D. Bind to an allosteric site to cause a conformational shift in the enzyme
Explanation
. Option D is correct since non-competitive inhibitors bind to a site on the enzyme away from the active site, called the allosteric site. The non-competitive inhibitors do not compete with the substrate for occupancy of the active site. The binding of the non-competitive inhibitor to the allosteric site brings about either a temporary or a permanent change in the shape of the active site Option A is incorrect since the inhibitors (both competitive and non-competitive) do not bind with the substrate. They bind with the enzyme. Option B is incorrect since the non-competitive inhibitor does not target the enzyme for destruction by a protease Option C is incorrect since it states the property of a competitive inhibitor
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Enzymes are biological catalysts that lower activation energy without being consumed, and their specificity is explained by the lock and key and induced fit models. Work includes the effects of temperature, pH and substrate concentration on reaction rate, plus competitive and non-competitive inhibition and how these differ.
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