1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data? d. What is the reason that humans are insensitive to sulfa drugs?
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data? d. What is the reason that humans are insensitive to sulfa drugs?
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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1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions.
a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain.
b. What prevents this enzyme from being an even more catalytically efficient enzyme?
c. What do single molecule data indicate about the validity of ensemble data?
d. What is the reason that humans are insensitive to sulfa drugs?
![| [S], mM | V, mM/sec (no inhibitor) | V, mM/sec (+inhibitor) | Reaction | Best fit line equation | Km or Km (app) | Vmax or Vmax (app) |
|---------|-------------------------|-----------------------|----------------|------------------------|----------------|---------------------|
| 0.5 | 12 | 5.5 | No inhibitor | | | |
| 2.0 | 20 | 9 | | | | |
| 5.0 | 29 | 13 | + inhibitor | | | |
| 13.5 | 35 | 16 | | | | |
| 45.0 | 40 | 18 | Type of inhibition | | | |
This table shows the effect of an enzyme inhibitor on the reaction rate at various substrate concentrations. The first column lists the substrate concentration ([S]) in mM. The second column shows the reaction rates (V) in mM/sec without an inhibitor, while the third column lists the reaction rates with an inhibitor present. The fourth column indicates whether a reaction involves an inhibitor or not.
The table leaves columns for the best fit line equation, Km or Km (app), and Vmax or Vmax (app) blank, suggesting further kinetic analysis is needed to determine these values. The type of inhibition is also to be identified.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F4bc2db8d-b0f4-497e-9433-81c9ca5ab613%2Fd26a9061-8b55-4eff-a008-c6c893ae8e28%2Fw5cwwmv_processed.png&w=3840&q=75)
Transcribed Image Text:| [S], mM | V, mM/sec (no inhibitor) | V, mM/sec (+inhibitor) | Reaction | Best fit line equation | Km or Km (app) | Vmax or Vmax (app) |
|---------|-------------------------|-----------------------|----------------|------------------------|----------------|---------------------|
| 0.5 | 12 | 5.5 | No inhibitor | | | |
| 2.0 | 20 | 9 | | | | |
| 5.0 | 29 | 13 | + inhibitor | | | |
| 13.5 | 35 | 16 | | | | |
| 45.0 | 40 | 18 | Type of inhibition | | | |
This table shows the effect of an enzyme inhibitor on the reaction rate at various substrate concentrations. The first column lists the substrate concentration ([S]) in mM. The second column shows the reaction rates (V) in mM/sec without an inhibitor, while the third column lists the reaction rates with an inhibitor present. The fourth column indicates whether a reaction involves an inhibitor or not.
The table leaves columns for the best fit line equation, Km or Km (app), and Vmax or Vmax (app) blank, suggesting further kinetic analysis is needed to determine these values. The type of inhibition is also to be identified.
Expert Solution
Step 1: Introduction
Enzyme kinetics:
The study of the reaction rates of enzyme catalyzed reactions.
- Initial reaction rate (at t = 0) is key and Vmax and Km can be determined.
- Useful for the determination of substrate specificity and reactions.
Chemical and enzymatic reactions take place at certain rates.
The rate is a measure of the rate of progress of the reaction as a function of time.
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