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]

Principles of Modern Chemistry

8th Edition

ISBN:9781305079113

Author:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler

Publisher:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler

Chapter18: Chemical Kinetics

Section: Chapter Questions

Problem 75AP

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Similar questions

Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
Compare the lock-and-key and induced-fit models for substrate binding to an enzyme.
List two ways that enzyme catalysis of a reaction is superior to normal conditions.
. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
When enzymes are present at very low concentration, their effect on reaction rate can be described by first-order kinetics. Calculate by what factor the rate of an enzyme-catalyzed reaction changes when the enzyme concentration is changed from 1.5 107 M to 4.5 106 M.