Multiple Choice
How can inhibitors prevent an enzyme from functioning normally?
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7. Enzyme Inhibition and Regulation
Enzyme Inhibition
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How does the shape of a competitive enzyme inhibitor determine its mechanism of inhibition?
A
It binds to an allosteric site, causing a conformational change in the enzyme.
B
It resembles the substrate, allowing it to bind to the active site and block substrate access.
C
It covalently modifies the enzyme, permanently inactivating it.
D
It increases the enzyme's affinity for the substrate by stabilizing the enzyme-substrate complex.
Verified step by step guidance1
Understand the concept of competitive inhibition: Competitive inhibitors are molecules that resemble the substrate of an enzyme and compete with the substrate for binding to the enzyme's active site.
Analyze the mechanism: Since competitive inhibitors mimic the substrate, they bind directly to the active site of the enzyme, preventing the actual substrate from binding and thus inhibiting the enzyme's activity.
Compare competitive inhibition with other types of inhibition: Competitive inhibitors do not bind to allosteric sites (non-active sites) or cause conformational changes in the enzyme. They also do not covalently modify the enzyme or permanently inactivate it.
Clarify the role of shape: The shape of a competitive inhibitor is crucial because it must closely resemble the substrate to fit into the enzyme's active site effectively. This structural similarity is the key to its mechanism of inhibition.
Conclude the mechanism: Competitive inhibitors block substrate access to the active site by occupying it, but they do not increase the enzyme's affinity for the substrate or stabilize the enzyme-substrate complex.
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