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What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?

What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?

Essentials Health Info Management Principles/Practices
Essentials Health Info Management Principles/Practices
4th Edition
ISBN:9780357191651
Author:Bowie
Publisher:Bowie
Chapter7: Numbering & Filing Systems And Record Storage & Circulation
Section7.5: Filing Controls
Problem 4E
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What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?
giupi unoulu 1UUK SImilar to the figure below. Michaelis Menten Plot.xls [Compatibility Mode] -Microsoft Excel Home Insert Page Layout Formulas Data Review View Add-Ins Acrobat Calibri 11 AA Insert- General Paste BIU- A. Delete Conditional Format Formatting- as Table Styles- $- % Cell EFormat- Clipboard G Font Alignment Number Styles Cells D24 A H K. 1 [Ethanol] Vo Calc. Vo delta^2 0.007 0.06 0.127403 0.004543 0.35 0.015 0.11 0.185644 0.005722 4 0.031 0.16 0.233942 0.005467 0. 0.068 0.21 0.26974 0.003569 0.25 6. 0.1 0.23 0.28128 0.00263 0.2 0.28 0.294674 0.000215 0.2 8 0.3 0.29 0.299427 8.89E-05 9 0.4 0.28 0.301861 0.000478 0.15 -Calc. Vo 10 0.022713 11 Km 0.01 0.1 12 Vmax 0.309407 0.05 13 14 16 0.1 0.2 0.3 0.4 0.5 17 18 Fig. 10. Michaelis-Menten Plot using a value of 0.01 mM for Km. Notice: 1) that a new set of calculated values in colum 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. 10 shows that the rates for the new enzyme-catalyzed reaction (red curve) were higher than those originally obtained (blue symbols).
Transcribed Image Text:giupi unoulu 1UUK SImilar to the figure below. Michaelis Menten Plot.xls [Compatibility Mode] -Microsoft Excel Home Insert Page Layout Formulas Data Review View Add-Ins Acrobat Calibri 11 AA Insert- General Paste BIU- A. Delete Conditional Format Formatting- as Table Styles- $- % Cell EFormat- Clipboard G Font Alignment Number Styles Cells D24 A H K. 1 [Ethanol] Vo Calc. Vo delta^2 0.007 0.06 0.127403 0.004543 0.35 0.015 0.11 0.185644 0.005722 4 0.031 0.16 0.233942 0.005467 0. 0.068 0.21 0.26974 0.003569 0.25 6. 0.1 0.23 0.28128 0.00263 0.2 0.28 0.294674 0.000215 0.2 8 0.3 0.29 0.299427 8.89E-05 9 0.4 0.28 0.301861 0.000478 0.15 -Calc. Vo 10 0.022713 11 Km 0.01 0.1 12 Vmax 0.309407 0.05 13 14 16 0.1 0.2 0.3 0.4 0.5 17 18 Fig. 10. Michaelis-Menten Plot using a value of 0.01 mM for Km. Notice: 1) that a new set of calculated values in colum 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. 10 shows that the rates for the new enzyme-catalyzed reaction (red curve) were higher than those originally obtained (blue symbols).
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