Multiple Choice
Which of the following statements is false regarding inhibitors & enzyme-catalyzed reactions?
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7. Enzyme Inhibition and Regulation
Enzyme Inhibition
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Which of the following best describes the action of a competitive inhibitor on an enzyme?
A
It binds to an allosteric site, increasing enzyme activity.
B
It irreversibly denatures the enzyme.
C
It binds to the active site, preventing substrate binding.
D
It binds to the substrate, enhancing its affinity for the enzyme.
Verified step by step guidance1
Understand the concept of enzyme inhibition: Enzyme inhibitors are molecules that reduce the activity of enzymes. Competitive inhibitors specifically compete with the substrate for binding to the enzyme's active site.
Recall the definition of a competitive inhibitor: A competitive inhibitor binds directly to the active site of the enzyme, preventing the substrate from binding. This type of inhibition is reversible and depends on the relative concentrations of the substrate and inhibitor.
Eliminate incorrect options: Analyze each option provided in the problem. For example, a competitive inhibitor does not bind to an allosteric site (this is characteristic of non-competitive inhibitors), nor does it irreversibly denature the enzyme (this is characteristic of irreversible inhibitors).
Focus on the correct mechanism: Competitive inhibitors mimic the substrate's structure and occupy the active site, effectively blocking substrate access. This reduces the rate of the enzyme-catalyzed reaction.
Summarize the correct answer: The best description of a competitive inhibitor is that it binds to the active site of the enzyme, preventing substrate binding and thereby reducing enzyme activity.
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