You have obtained experimental kinetic data for two versions of the same enzyme, a wild-type and a mutant differing from the wild-type at a single amino acid. The data are given in the table. Vmax KM (µmol min-1) (mM) Wild-type 100 10 Mutant 1 0.1 Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which k-j is much larger than k2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild-type version requires a greater concentration of substrate to achieve Vmax - The wild-type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve Vmax -
You have obtained experimental kinetic data for two versions of the same enzyme, a wild-type and a mutant differing from the wild-type at a single amino acid. The data are given in the table. Vmax KM (µmol min-1) (mM) Wild-type 100 10 Mutant 1 0.1 Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which k-j is much larger than k2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild-type version requires a greater concentration of substrate to achieve Vmax - The wild-type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve Vmax -
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
Related questions
Question
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table.
Compare the kinetic parameters of the two versions using the data in the table.
Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct?
- The mutant version has a higher affinity for the substrate.
- The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax.
- The wild‑type version has a higher affinity for the substrate.
- The mutant version requires a greater concentration of substrate to achieve ?maxVmax.
Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM.
The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product.
Based on the data table and your initial velocity calculation, the reaction equilibrium is altered more in the direction of the product by
- wild type version
- mutant version
- neither version
- both versions

Transcribed Image Text:You have obtained experimental kinetic data for two versions of the same enzyme, a wild-type and a mutant differing from the
wild-type at a single amino acid. The data are given in the table.
Vmax
Км
(µmol min-1)
(mM)
Wild-type
100
10
Mutant
1
0.1
Compare the kinetic parameters of the two versions using the data in the table.
Assuming a two-step reaction scheme in which k_j is much larger than k2, which of the following statements are correct?
The mutant version has a higher affinity for the substrate.
The wild-type version requires a greater concentration of substrate to achieve Vmax -
The wild-type version has a higher affinity for the substrate.
The mutant version requires a greater concentration of substrate to achieve Vmax ·

Transcribed Image Text:Calculate the initial velocity of the reaction catalyzed by the wild-type enzyme when the substrate concentration is 10 mM.
-1
Vo
µmol min
The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product.
Based on the data table and your initial velocity calculation, the reaction equilibrium is altered more in the direction of the
product by
the wild-type version.
the mutant version.
neither version.
both versions.
Expert Solution

This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 4 steps

Recommended textbooks for you

Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman

Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY

Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman

Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY

Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning

Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning

Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON