Multiple Choice
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.
7. Enzyme Inhibition and Regulation
Uncompetitive Inhibition
Struggling with Biochemistry?
Join thousands of students who trust us to help them ace their exams!Watch the first videoMultiple Choice
True or false: Increasing [S] in the presence of an uncompetitive inhibitor will lower the inhibition constant (KI).
A
True.
B
False.
Verified step by step guidance1
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.
4:57mWatch next
Master Uncompetitive Inhibition with a bite sized video explanation from Jason
Start learningRelated Videos
Related Practice
Uncompetitive Inhibition practice set
Problem sets built by lead tutorsExpert video explanations