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he kinetics of an enzyme-catalyzed reaction is measured in the absence and presence of two potential inhibitors (A and B). n experiements involving inhibitors concentrations of 9.8 mM. Substrate No Inhibitor Inhibitor A Inhibitor B (S]/M V o/M s-1 vo/M s-1 vo/M s-1 5.00E-04 1.26E-06 5.83E-07 3.83E-07 1.00E-03 2.01E-06 1.04E-06 6.34E-07 2.50E-03 3.12E-06 2.00E-06 9.99E-07 5.00E-03 3.85E-06 2.78E-06 1.25E-06 1.00E-02 4.54E-06 3.57E-06 1.43E-06 From these date, determine the values of KM and Vmax fo the enzyme. For the inhibitors, determine the type of inhibition, by creating a Lineweaver-Burk plot comparing all three experiments For each inhibitor, the inhibitor constant Ki = [ES][1)/[ESI]

he kinetics of an enzyme-catalyzed reaction is measured in the absence and presence of two potential inhibitors (A and B). n experiements involving inhibitors concentrations of 9.8 mM. Substrate No Inhibitor Inhibitor A Inhibitor B (S]/M V o/M s-1 vo/M s-1 vo/M s-1 5.00E-04 1.26E-06 5.83E-07 3.83E-07 1.00E-03 2.01E-06 1.04E-06 6.34E-07 2.50E-03 3.12E-06 2.00E-06 9.99E-07 5.00E-03 3.85E-06 2.78E-06 1.25E-06 1.00E-02 4.54E-06 3.57E-06 1.43E-06 From these date, determine the values of KM and Vmax fo the enzyme. For the inhibitors, determine the type of inhibition, by creating a Lineweaver-Burk plot comparing all three experiments For each inhibitor, the inhibitor constant Ki = [ES][1)/[ESI]

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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The kinetics of an enzyme-catalyzed reaction is measured in the absence and presence of two potential inhibitors (A and B). In experiements involving inhibitors concentrations of 9.8 mM. Substrate No Inhibitor Inhibitor A Inhibitor B [S]/M V o/M s-1 vo/M s-1 vo/M s-1 5.00E-04 1.26E-06 5.83E-07 3.83E-07 1.00E-03 2.01E-06 1.04E-06 6.34E-07 2.50E-03 3.12E-06 2.00E-06 9.99E-07 5.00E-03 3.85E-06 2.78E-06 1.25E-06 1.00E-02 4.54E-06 3.57E-06 1.43E-06 From these date, determine the values of KM and Vmax fo the enzyme. For the inhibitors, determine the type of inhibition, by creating a Lineweaver-Burk plot comparing all three experiments. For each inhibitor, the inhibitor constant Ki = [ES][I]/[ESI]
Transcribed Image Text:The kinetics of an enzyme-catalyzed reaction is measured in the absence and presence of two potential inhibitors (A and B). In experiements involving inhibitors concentrations of 9.8 mM. Substrate No Inhibitor Inhibitor A Inhibitor B [S]/M V o/M s-1 vo/M s-1 vo/M s-1 5.00E-04 1.26E-06 5.83E-07 3.83E-07 1.00E-03 2.01E-06 1.04E-06 6.34E-07 2.50E-03 3.12E-06 2.00E-06 9.99E-07 5.00E-03 3.85E-06 2.78E-06 1.25E-06 1.00E-02 4.54E-06 3.57E-06 1.43E-06 From these date, determine the values of KM and Vmax fo the enzyme. For the inhibitors, determine the type of inhibition, by creating a Lineweaver-Burk plot comparing all three experiments. For each inhibitor, the inhibitor constant Ki = [ES][I]/[ESI]
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