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In the presence of an uncompetitive inhibitor that binds __________ the substrate, the apparent Vmax ____________ and the apparent Km ____________ with respect to the Vmax and Km of the uninhibited enzyme.
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7. Enzyme Inhibition and Regulation
Uncompetitive Inhibition
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True or false: Increasing [S] in the presence of an uncompetitive inhibitor will lower the inhibition constant (KI).
A
True.
B
False.
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Understand the role of an uncompetitive inhibitor: An uncompetitive inhibitor binds only to the enzyme-substrate complex, not to the free enzyme. This binding decreases the overall number of active enzyme-substrate complexes available for the reaction.
Consider the effect of substrate concentration ([S]): In the presence of an uncompetitive inhibitor, increasing the substrate concentration ([S]) leads to more enzyme-substrate complexes, which can be bound by the inhibitor.
Analyze the inhibition constant (KI): The inhibition constant (KI) is a measure of the affinity of the inhibitor for the enzyme-substrate complex. It is not directly affected by changes in substrate concentration.
Evaluate the relationship between [S] and KI: Since KI is a constant that describes the binding affinity of the inhibitor, it remains unchanged regardless of the substrate concentration. Increasing [S] does not lower KI.
Conclude the statement: Based on the understanding of uncompetitive inhibition and the nature of KI, the statement 'Increasing [S] in the presence of an uncompetitive inhibitor will lower the inhibition constant (KI)' is false.
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