For an enzyme catalyzed reaction, the presence of 5nM of a reversible inhibitor yields a Vmax value equals to that measured in the absence of the inhibitor. However, the KM value was increased by a factor of two compared to the KM measured in the absence of the inhibitor. - What type of inhibition is likely occurring? - How is the affinity modified in the presence of the inhibitor? - Calculate the inhibition constant.

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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For an enzyme catalyzed reaction, the presence of 5nM of a reversible inhibitor yields a Vmax value
equals to that measured in the absence of the inhibitor. However, the KM value was increased by a factor
of two compared to the KM measured in the absence of the inhibitor.
- What type of inhibition is likely occurring?
- How is the affinity modified in the presence of the inhibitor?
- Calculate the inhibition constant.
Transcribed Image Text:For an enzyme catalyzed reaction, the presence of 5nM of a reversible inhibitor yields a Vmax value equals to that measured in the absence of the inhibitor. However, the KM value was increased by a factor of two compared to the KM measured in the absence of the inhibitor. - What type of inhibition is likely occurring? - How is the affinity modified in the presence of the inhibitor? - Calculate the inhibition constant.
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