Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059
Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059
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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![Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5)
Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and
fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have
prepared five different concentrations of substrate (sucrose), and five different concentrations of
inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the
inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.)
for all six of these experiments:
1/ V.
(1)
0 mM
O mM
0 mM
0 mM
0 mM
[S]
0.1 mM
0.2 mM
Vo
0.3333
0.50
1/[S]
33333 mM per minute
0.3 mM
0.4 mM
0.5 mM
0.60
0.666666666667
0.714285714286
0.1 mM
0.1 mM
0.20
0.2 mM
0.3 mM
0.1 mM
0.333333333333
0.428571428571
0.50
0.1 mM
0.1 mM
0.4 mM
0.5 mM
0.1 mM
0.1 mM
0.555555555556
0.20 mM
0.20 mM
0.20 mM
0.20 mM
0.20 mM
0.3 mM
0.142857142857
0.25
0.2 mM
0.3 mM
0.333333333333
0.40
0.454545454545
0.111111111111
0.20
0.4 mM
0.5 mM
0.1 mM
0.2 mM
0.3 mM
0.4 mM
0.5 mM
0.1 mM
0.3 mM
0.272727272727
0.333333333333
0.384615384615
0.3 mM
0.3 mM
0.3 mM
0.40 mM
0.090909090909
0.40 mM
0.40 mM
0.40 mM
0.40 mM
0.5 mM
0.5 mM
0.2 mM
0.3 mM
0.4 mM
0.5 mM
0.1 mM
0.2 mM
0.3 mM
0.4 mM
0.166666666667
0.230769230769
0.285714285714
0.333333333333
0.076923076923
0.142857142857.
0.20
0.25
0.5 mM
0.5 mM
0.5 mM
Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments
on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the
control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3,
0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A?
0.5 mM
0.294117647059](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F1aa73a5c-541c-4668-bc8d-58d278629b47%2F2cd97f56-bef3-4f6d-9675-510fd6c3aa1b%2Fqkhee9t.jpeg&w=3840&q=75)
Transcribed Image Text:Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5)
Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and
fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have
prepared five different concentrations of substrate (sucrose), and five different concentrations of
inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the
inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.)
for all six of these experiments:
1/ V.
(1)
0 mM
O mM
0 mM
0 mM
0 mM
[S]
0.1 mM
0.2 mM
Vo
0.3333
0.50
1/[S]
33333 mM per minute
0.3 mM
0.4 mM
0.5 mM
0.60
0.666666666667
0.714285714286
0.1 mM
0.1 mM
0.20
0.2 mM
0.3 mM
0.1 mM
0.333333333333
0.428571428571
0.50
0.1 mM
0.1 mM
0.4 mM
0.5 mM
0.1 mM
0.1 mM
0.555555555556
0.20 mM
0.20 mM
0.20 mM
0.20 mM
0.20 mM
0.3 mM
0.142857142857
0.25
0.2 mM
0.3 mM
0.333333333333
0.40
0.454545454545
0.111111111111
0.20
0.4 mM
0.5 mM
0.1 mM
0.2 mM
0.3 mM
0.4 mM
0.5 mM
0.1 mM
0.3 mM
0.272727272727
0.333333333333
0.384615384615
0.3 mM
0.3 mM
0.3 mM
0.40 mM
0.090909090909
0.40 mM
0.40 mM
0.40 mM
0.40 mM
0.5 mM
0.5 mM
0.2 mM
0.3 mM
0.4 mM
0.5 mM
0.1 mM
0.2 mM
0.3 mM
0.4 mM
0.166666666667
0.230769230769
0.285714285714
0.333333333333
0.076923076923
0.142857142857.
0.20
0.25
0.5 mM
0.5 mM
0.5 mM
Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments
on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the
control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3,
0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A?
0.5 mM
0.294117647059
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