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] - MicrosatHomeInsertPage LayoutFormulasDataReviewViewAdd-InsAcrobat* CutCalibri11CopyWrap TextGeneralPasteBFormat PainterE Merge & Center -14A Conditional FormaFormatting as TablS4-%ClipboardFontAlignmentNumberC16AB.D.F.GJ.HK.1 [Ethanol]VoCalc. Vo delta^220.0070.060.037997 0.0004840.353.0.0150.110.0714020.0014940.0310.160.118415 0.00172903150.0680.210.178303 0.0010050.10.230.206272 0.0005630.2570.20.280.247526 0.0010550.20.30.290.265206 0.000615• vo0.40.280.275029 2.47E-050.15Calc. Vo100.00696511Km0.050.112Vmax0.3094070.051314160.10.20.30.40.51718Fig. 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 and2) 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) aregenerally lower than those originally obtained (blue symbols). Bookl.xls [Compatibility Mode] - Microsoft ExcelHomeInsertPage LayoutFormulasDataReviewViewAdd-InsAcrobatGeneralConditional FormattingInsert-DeleteCalibri-11A AS- %Format as Table-PasteBI U8 98ECell StylesFormat-Sort &FilterClipboardFontAlignmentNumberStylesCellsEditirH20fxBDEGHKM1 [Ethanol]VoCalc. Vo delta^22.0.0070.060.059516 2.35E-070.350.0150.110.10455 2.97E-050.34.0.0310.160.158825 1.38E-060.0680.210.216033 3.64E-050.250.10.230.239125 8.33E-057.0.20.280.269764 0.0001050.2• Vo0.30.290.281799 6.73E-059.0.40.280.288229 6.77E-050.15Calc. Vo100.0003910.111Km0.02939112Vmax0.3094070.0513140.10.20.30.40.5161718Fig. 7. Final Michaelis-Menten Plot.

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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
Home
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General
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14A Conditional Forma
Formatting as Tabl
S4-%
Clipboard
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Alignment
Number
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
Home
Insert
Page Layout
Formulas
Data
Review
View
Add-Ins
Acrobat
General
Conditional Formatting
Insert-
Delete
Calibri
-11
A A
S- %
Format as Table-
Paste
B
I U
8 98
ECell Styles
Format-
Sort &
Filter
Clipboard
Font
Alignment
Number
Styles
Cells
Editir
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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Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?
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An enzyme with a low Km is considered to have a higher affinity for the substrate. Provide explanations.
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Describe the specific multi-enzyme example discussed in class of how enzyme activity can be altered by changing its substrate to product ratio.
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Does the presence of an uncompetitive inhibitor increase / decrease the apparent affinity of the enzyme•substrate complex?Does the apparent KM increase / decrease in the presence of an uncompetitive inhibitor?
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.