7. A group of Colby students discovered a hydrolase that cleaves cellulose. After purifying the enzyme, an assay was performed by adding 0.1 µM of enzyme to the cellulose substrate concentrations shown below to characterize kinetic properties. [S] 2 x 10-6 M 4 x 10-6 1 x 10-5 2 x 10-5 4 x 10-5 1 x 10-4 2 x 10-³ 1 x 10-² 4 x 10-² V (umol/min) 28 40 75 95 112 128 139 140 141 A. Use the data in the table above to estimate KM and B. What is the keat of this enzyme? C. What is the catalytic efficiency of this enzyme? Max for the enzyme.

7. A group of Colby students discovered a hydrolase that cleaves cellulose. After purifying the enzyme, an assay was performed by adding 0.1 µM of enzyme to the cellulose substrate concentrations shown below to characterize kinetic properties. [S] 2 x 10-6 M 4 x 10-6 1 x 10-5 2 x 10-5 4 x 10-5 1 x 10-4 2 x 10-³ 1 x 10-² 4 x 10-² V (umol/min) 28 40 75 95 112 128 139 140 141 A. Use the data in the table above to estimate KM and B. What is the keat of this enzyme? C. What is the catalytic efficiency of this enzyme? Max for the enzyme.

Chemistry & Chemical Reactivity

9th Edition

ISBN:9781133949640

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter24: Biochemistry

Section: Chapter Questions

Problem 35IL

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Similar questions

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 difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
. 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?
The Arrhenius equation quantifies which of the following effects? the pre-orientation effect in heterogeneous catalysts temperature increasing the percent of successful collisions substrate concentration in enzyme-catalyzed reactions O pressure increasing the overall number of collisions activation energy reduction in homogeneous catalysts
7TA Which of the following is not true regarding enzymes? * They catalyze only a particular type of reaction They are destroyed after the completion of the reaction they catalyse They remain active even after separation from the source Their activity depends on the pH of the solution Which of these statements about enzyme- catalyzed reactions is true? * The activation energy for the catalyzed O reaction is the same as for the uncatalyzed reaction. The rate of a reaction decreases steadily with time as substrate is depleted. At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is propeE
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] U = Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. 300 V Next, move the line labeled 1/2 Vmax to its correct position. max 275 Then, move the line labeled Km to its correct position. 250 225 200 175 Michaelis–Menten curve 150 K a 125 m 100 1/2 V 75 max 50 25 10 20 30 40 50 60 70 80 90 100 [S] (µM) Incorrect Estimate the values for Vmax and Km. Vmax 175 µM/min Km 14 µM v (µM/min)