What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?
What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?
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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Question
What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?
![Michaelis Menten Plot.ls (Compatibility Mode] - Microsat
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C16
A
B.
D.
F.
G
J.
H
K.
1 [Ethanol]
Vo
Calc. Vo delta^2
2
0.007
0.06
0.037997 0.000484
0.35
3.
0.015
0.11
0.071402
0.00149
4
0.031
0.16
0.118415 0.001729
03
15
0.068
0.21
0.178303 0.001005
0.1
0.23
0.206272 0.000563
0.25
7
0.2
0.28
0.247526 0.001055
0.2
0.3
0.29
0.265206 0.000615
• vo
0.4
0.28
0.275029 2.47E-05
0.15
Calc. Vo
10
0.006965
11
Km
0.05
0.1
12
Vmax
0.309407
0.05
13
14
16
0.1
0.2
0.3
0.4
0.5
17
18
Fig. 8. Michaelis-Menten Plot using a value of 0.05 mM for Km.
Notice: 1) that a new set of calculated values in column C has been generated and
2) that by using these new data a new best fit Michaelis-Menten plot (red curve)
has been generated.
Fig. 8 shows that the rates for the new enzyme-catalyzed reaction (red curve) are
generally lower than those originally obtained (blue symbols).](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F5ef5f725-b08b-4f71-a80c-f37e47d07785%2Fef8f44fb-ad00-4cfd-b9ab-dd7961a0e5ac%2Fxjj1a8m_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Michaelis Menten Plot.ls (Compatibility Mode] - Microsat
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C16
A
B.
D.
F.
G
J.
H
K.
1 [Ethanol]
Vo
Calc. Vo delta^2
2
0.007
0.06
0.037997 0.000484
0.35
3.
0.015
0.11
0.071402
0.00149
4
0.031
0.16
0.118415 0.001729
03
15
0.068
0.21
0.178303 0.001005
0.1
0.23
0.206272 0.000563
0.25
7
0.2
0.28
0.247526 0.001055
0.2
0.3
0.29
0.265206 0.000615
• vo
0.4
0.28
0.275029 2.47E-05
0.15
Calc. Vo
10
0.006965
11
Km
0.05
0.1
12
Vmax
0.309407
0.05
13
14
16
0.1
0.2
0.3
0.4
0.5
17
18
Fig. 8. Michaelis-Menten Plot using a value of 0.05 mM for Km.
Notice: 1) that a new set of calculated values in column C has been generated and
2) that by using these new data a new best fit Michaelis-Menten plot (red curve)
has been generated.
Fig. 8 shows that the rates for the new enzyme-catalyzed reaction (red curve) are
generally lower than those originally obtained (blue symbols).
![Bookl.xls [Compatibility Mode] - Microsoft Excel
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H20
fx
B
D
E
G
H
K
M
1 [Ethanol]
Vo
Calc. Vo delta^2
2.
0.007
0.06
0.059516 2.35E-07
0.35
0.015
0.11
0.10455 2.97E-05
0.3
4.
0.031
0.16
0.158825 1.38E-06
0.068
0.21
0.216033 3.64E-05
0.25
0.1
0.23
0.239125 8.33E-05
7.
0.2
0.28
0.269764 0.000105
0.2
• Vo
0.3
0.29
0.281799 6.73E-05
9.
0.4
0.28
0.288229 6.77E-05
0.15
Calc. Vo
10
0.000391
0.1
11
Km
0.029391
12
Vmax
0.309407
0.05
13
14
0.1
0.2
0.3
0.4
0.5
16
17
18
Fig. 7. Final Michaelis-Menten Plot.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F5ef5f725-b08b-4f71-a80c-f37e47d07785%2Fef8f44fb-ad00-4cfd-b9ab-dd7961a0e5ac%2Fhbkm7s_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Bookl.xls [Compatibility Mode] - Microsoft Excel
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H20
fx
B
D
E
G
H
K
M
1 [Ethanol]
Vo
Calc. Vo delta^2
2.
0.007
0.06
0.059516 2.35E-07
0.35
0.015
0.11
0.10455 2.97E-05
0.3
4.
0.031
0.16
0.158825 1.38E-06
0.068
0.21
0.216033 3.64E-05
0.25
0.1
0.23
0.239125 8.33E-05
7.
0.2
0.28
0.269764 0.000105
0.2
• Vo
0.3
0.29
0.281799 6.73E-05
9.
0.4
0.28
0.288229 6.77E-05
0.15
Calc. Vo
10
0.000391
0.1
11
Km
0.029391
12
Vmax
0.309407
0.05
13
14
0.1
0.2
0.3
0.4
0.5
16
17
18
Fig. 7. Final Michaelis-Menten Plot.
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