Table 1 shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme concentration, [E]r, is the same for each experiment. Table 1 [S] (mM) Vo Vo {umol/(mL•s)} {umol/(mL•s)} Without Inhibitor With Inhibitor (1) 3.8 (2) 2.2 1 7.3 13.3 22.9 4.3 4 8.2 8 14.9 12 30.0 20.4
Table 1 shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme concentration, [E]r, is the same for each experiment. Table 1 [S] (mM) Vo Vo {umol/(mL•s)} {umol/(mL•s)} Without Inhibitor With Inhibitor (1) 3.8 (2) 2.2 1 7.3 13.3 22.9 4.3 4 8.2 8 14.9 12 30.0 20.4
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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Answer bi) and bii) only
![Table 1 shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in
the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme
concentration, [E]T, is the same for each experiment.
Table 1
[S]
(mM)
Vo
Vo
{umol/(mL•s)}
{umol/(mL•s)}
Without Inhibitor
With Inhibitor
(1)
3.8
(2)
2.2
1
7.3
4.3
4
13.3
8.2
8
22.9
14.9
12
30.0
20.4
a)
Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1.
a)
Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.
b) i
Determine the type of inhibition.
Determine the dissociation constant, K;, for the inhibitor binding to the enzyme. Show
your working.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F07aa9f75-e89d-44f8-bb0f-9c115d09f79e%2Fad86da05-97f7-4be9-a8e8-14b234059eb6%2Fk8mq16m_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Table 1 shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in
the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme
concentration, [E]T, is the same for each experiment.
Table 1
[S]
(mM)
Vo
Vo
{umol/(mL•s)}
{umol/(mL•s)}
Without Inhibitor
With Inhibitor
(1)
3.8
(2)
2.2
1
7.3
4.3
4
13.3
8.2
8
22.9
14.9
12
30.0
20.4
a)
Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1.
a)
Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.
b) i
Determine the type of inhibition.
Determine the dissociation constant, K;, for the inhibitor binding to the enzyme. Show
your working.
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