What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?

Essentials Health Info Management Principles/Practices
4th Edition
ISBN:9780357191651
Author:Bowie
Publisher:Bowie
Chapter10: Introduction To Coding And Reimbursement
Section10.1: Clinical Classification Systems
Problem 5E
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What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
Michaelis Menten Plot.ds (Compatibility Mode] - Microsoft Excel
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F24
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B
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H
M
1 [Ethanol)
Vo
Calc. Vo delta^2
0.007
0.06
0.0327 0.000745
0.35
3
0.015
0.11
0.057444 0.002762
4.
0.031
0.16
0.087264
0.00529
0.3
0.068
0.21
0.118696 0.008336
0.1
0.23
0.131384 0.009725
0.25
0.2
0.28
0.148218 0.017366
0.2
0.3
0.29
0.154831 0.018271
• Vo
0.4
0.28
0.158364 0.014795
0.15
Calc. Vo
10
0.077292
11
Km
0.029391
0.1
12
Vmax
0.17
0.05
13
14
16
0.1
0.2
03
0.4
0.5
17
18
Fig. 11. Michaelis-Menten Plot using a value of 0.17 for Vmax.
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. 11 shows that the rates for the new enzyme-catalyzed reaction (red curve) are
significantly lower than those originally obtained (blue symbols).
Transcribed Image Text:Michaelis Menten Plot.ds (Compatibility Mode] - Microsoft Excel Home Insert Page Layout Formulas Data Review View Add-Ins Acrobat Calibri 11 Insert - General Paste Delete - Conditional Format Cell Clipboard Formatting- as Table Styles- Format- Font Alignment Number Styles Cells F24 A B D G H M 1 [Ethanol) Vo Calc. Vo delta^2 0.007 0.06 0.0327 0.000745 0.35 3 0.015 0.11 0.057444 0.002762 4. 0.031 0.16 0.087264 0.00529 0.3 0.068 0.21 0.118696 0.008336 0.1 0.23 0.131384 0.009725 0.25 0.2 0.28 0.148218 0.017366 0.2 0.3 0.29 0.154831 0.018271 • Vo 0.4 0.28 0.158364 0.014795 0.15 Calc. Vo 10 0.077292 11 Km 0.029391 0.1 12 Vmax 0.17 0.05 13 14 16 0.1 0.2 03 0.4 0.5 17 18 Fig. 11. Michaelis-Menten Plot using a value of 0.17 for Vmax. 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. 11 shows that the rates for the new enzyme-catalyzed reaction (red curve) are significantly lower than those originally obtained (blue symbols).
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