Multiple Choice
True or false: Increasing [S] in the presence of an uncompetitive inhibitor will lower the inhibition constant (KI).
7. Enzyme Inhibition and Regulation
Uncompetitive Inhibition
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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.
A
Before, Decreases, Increases.
B
After, Decreases, Decreases.
C
After, Increases, Increases.
D
Before, Stays the same, Decreases.
E
After, Decreases, Stays the same.
Verified step by step guidance1
Understand the concept of enzyme inhibition: Uncompetitive inhibitors bind to the enzyme-substrate complex, not the free enzyme. This affects both the Vmax and Km values.
Identify the effect of uncompetitive inhibition on Vmax: Uncompetitive inhibitors decrease the apparent Vmax because they prevent the enzyme from converting substrate to product efficiently.
Identify the effect of uncompetitive inhibition on Km: Uncompetitive inhibitors also decrease the apparent Km because they stabilize the enzyme-substrate complex, making it seem like the enzyme has a higher affinity for the substrate.
Consider the timing of inhibitor binding: Uncompetitive inhibitors bind after the substrate has bound to the enzyme, forming the enzyme-substrate complex.
Match the correct answer with the effects: The correct answer should reflect that uncompetitive inhibitors bind after the substrate, decrease the apparent Vmax, and decrease the apparent Km.
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