3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹ M, the following data were obtained. [CO2]o (M) 0.00125 0.00250 0.00500 0.02000 v (M/s) 2.78 x 10-5 5.00 x 10-5 8.33 x 10-5 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹ M, the following data were obtained. [CO2]o (M) 0.00125 0.00250 0.00500 0.02000 v (M/s) 2.78 x 10-5 5.00 x 10-5 8.33 x 10-5 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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![3. **Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation.**
The hydration of CO₂ is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10⁻⁹ M, the following data were obtained:
| [CO₂]₀ (M) | v (M/s) |
|--------------|--------------|
| 0.00125 | 2.78 x 10⁻⁵ |
| 0.00250 | 5.00 x 10⁻⁵ |
| 0.00500 | 8.33 x 10⁻⁵ |
| 0.02000 | 1.66 x 10⁻⁴ |
Plot these according to the Burke-Lineweaver Equation and determine the values of Kₘ, the Michaelis constant, and k₂, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ff6ab806b-464c-4756-9d8f-72da0489465e%2F0acbd447-660d-465e-a4c7-3e3e913eb989%2F0zuv5v8_processed.png&w=3840&q=75)
Transcribed Image Text:3. **Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation.**
The hydration of CO₂ is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10⁻⁹ M, the following data were obtained:
| [CO₂]₀ (M) | v (M/s) |
|--------------|--------------|
| 0.00125 | 2.78 x 10⁻⁵ |
| 0.00250 | 5.00 x 10⁻⁵ |
| 0.00500 | 8.33 x 10⁻⁵ |
| 0.02000 | 1.66 x 10⁻⁴ |
Plot these according to the Burke-Lineweaver Equation and determine the values of Kₘ, the Michaelis constant, and k₂, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
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