What conclusion can be drawn concerning an inhibitor if Vmax is the same in the presence and absence of the inhibitor? a. KM is smaller in the presence of the inhibitor. Ob. The inhibitor binds to the same active site as the substrate. Oc. The inhibitor binds to the substrate. Od. The inhibitor reacts with a critical residue of the enzyme. Je. The inhibitor can be overcome with sufficiently high concentrations of the substrate.
What conclusion can be drawn concerning an inhibitor if Vmax is the same in the presence and absence of the inhibitor? a. KM is smaller in the presence of the inhibitor. Ob. The inhibitor binds to the same active site as the substrate. Oc. The inhibitor binds to the substrate. Od. The inhibitor reacts with a critical residue of the enzyme. Je. The inhibitor can be overcome with sufficiently high concentrations of the substrate.
Chemistry for Today: General, Organic, and Biochemistry
9th Edition
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Chapter20: Enzymes
Section: Chapter Questions
Problem 20.75E: In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent...
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