Q6. You measure the kinetics of an enzyme as a function of substrate concentration, first without any inhibitor and then in the presence of 10.0 mM inhibitor A and 10.0 mM inhibitor B. The enzyme concentration is maintained constant at a level of 2.00 μM. [S] (μM) v (μM/min) no inhibitor v (μM/min) 10.0 mM A v (μM/min) 10.0 mM B 2 2.86 2.50 0.91 4 4.44 3.64 1.67 5 5.00 4.00 2.00 10 6.67 5.00 3.33 a. From these data, determine Vm, Km and the turnover number (kcat) for the enzyme. b. From these data determine the type of inhibition for inhibitor A and inhibitor B. c. Which of the inhibitors is more effective at high substrate concentrations? Explain your reasoning. d. Determine the dissociation constant Ki (or Ki) for each of the inhibitors.
Q6. You measure the kinetics of an enzyme as a function of substrate concentration, first without any inhibitor and then in the presence of 10.0 mM inhibitor A and 10.0 mM inhibitor B. The enzyme concentration is maintained constant at a level of 2.00 μM. [S] (μM) v (μM/min) no inhibitor v (μM/min) 10.0 mM A v (μM/min) 10.0 mM B 2 2.86 2.50 0.91 4 4.44 3.64 1.67 5 5.00 4.00 2.00 10 6.67 5.00 3.33 a. From these data, determine Vm, Km and the turnover number (kcat) for the enzyme. b. From these data determine the type of inhibition for inhibitor A and inhibitor B. c. Which of the inhibitors is more effective at high substrate concentrations? Explain your reasoning. d. Determine the dissociation constant Ki (or Ki) for each of the inhibitors.
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
Section: Chapter Questions
Problem 1P
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Please atleast answer this question ?
![You measure the kinetics of an enzyme as a function of substrate
concentration, first without any inhibitor and then in the presence of 10.0 mM inhibitor A
and 10.0 mM inhibitor B. The enzyme concentration is maintained constant at a level of
2.00 μM.
[S] (μm)
Q6.
2
4
5
10
v (μM/min)
no inhibitor
2.86
4.44
5.00
6.67
v (μM/min)
10.0 mM A
2.50
3.64
4.00
5.00
v (μM/min)
10.0 mM B
0.91
1.67
2.00
3.33
a. From these data, determine Vm, Km and the turnover number (kcar) for the enzyme.
b. From these data determine the type of inhibition for inhibitor A and inhibitor B.
c. Which of the inhibitors is more effective at high substrate concentrations? Explain
your reasoning.
d. Determine the dissociation constant Ki (or Ki) for each of the inhibitors.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fe2a1ef0b-51c8-4819-88dd-b00cf8efbd62%2Fbca49832-0906-4758-84b3-30b382519514%2Fwf4769r_processed.png&w=3840&q=75)
Transcribed Image Text:You measure the kinetics of an enzyme as a function of substrate
concentration, first without any inhibitor and then in the presence of 10.0 mM inhibitor A
and 10.0 mM inhibitor B. The enzyme concentration is maintained constant at a level of
2.00 μM.
[S] (μm)
Q6.
2
4
5
10
v (μM/min)
no inhibitor
2.86
4.44
5.00
6.67
v (μM/min)
10.0 mM A
2.50
3.64
4.00
5.00
v (μM/min)
10.0 mM B
0.91
1.67
2.00
3.33
a. From these data, determine Vm, Km and the turnover number (kcar) for the enzyme.
b. From these data determine the type of inhibition for inhibitor A and inhibitor B.
c. Which of the inhibitors is more effective at high substrate concentrations? Explain
your reasoning.
d. Determine the dissociation constant Ki (or Ki) for each of the inhibitors.
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