Homework Help is Here – Start Your Trial Now!
Science
Biochemistry
(a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.

(a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.

Biochemistry
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
See similar textbooks
icon
Related questions
Question
100%

Michaelis-Menten Plot Problem Help

 

See Picture

**Michaelis-Menten Plot Analysis of WT and Mutant (V105A) Enzymes** Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium *Staphylococcus aureus*. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. ### Graph Description: - **Axes:** The x-axis represents substrate concentration \([S]\) in mM, ranging from 0 to 500 mM. The y-axis represents the reaction velocity \(v\) in \(\mu \text{mol} \, \text{s}^{-1} \, \text{mg}^{-1}\) of enzyme, ranging from 0.00 to 1.50 \(\mu \text{mol} \, \text{s}^{-1} \, \text{mg}^{-1}\). - **Curves:** - The black curve represents the WT enzyme. - The red curve represents the mutant V105A enzyme. - **Data Points:** Each curve has data points with error bars indicating variability in the measurements. ### Questions: (a) **Estimate the \(K_m\) and \(V_{max}\) for the wild-type and mutant enzyme from the graph.** (b) **Calculate the \(K_{cat}\) and \(K_{cat}/K_m\) for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 \(\mu \text{mol/mg}\).** (c) **Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.** ### Analysis Approach: - **Estimate \(V_{max}\):** Look for the plateau of each curve to identify \(V_{max}\). - **Estimate \(K_m\):** Find the substrate concentration where the reaction velocity is half of \(V_{max}\). - **Calculate \(K_{cat}\):** Use the formula \(K_{cat} = \frac{V_{max}}{[E_t]}\), where \([E_t]\) is the total enzyme concentration. - **Determine Efficiency:** Assess the catalytic efficiency using \(K_{cat}/K_m\) and compare between the WT and mutant enzymes.
Transcribed Image Text:**Michaelis-Menten Plot Analysis of WT and Mutant (V105A) Enzymes** Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium *Staphylococcus aureus*. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. ### Graph Description: - **Axes:** The x-axis represents substrate concentration \([S]\) in mM, ranging from 0 to 500 mM. The y-axis represents the reaction velocity \(v\) in \(\mu \text{mol} \, \text{s}^{-1} \, \text{mg}^{-1}\) of enzyme, ranging from 0.00 to 1.50 \(\mu \text{mol} \, \text{s}^{-1} \, \text{mg}^{-1}\). - **Curves:** - The black curve represents the WT enzyme. - The red curve represents the mutant V105A enzyme. - **Data Points:** Each curve has data points with error bars indicating variability in the measurements. ### Questions: (a) **Estimate the \(K_m\) and \(V_{max}\) for the wild-type and mutant enzyme from the graph.** (b) **Calculate the \(K_{cat}\) and \(K_{cat}/K_m\) for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 \(\mu \text{mol/mg}\).** (c) **Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.** ### Analysis Approach: - **Estimate \(V_{max}\):** Look for the plateau of each curve to identify \(V_{max}\). - **Estimate \(K_m\):** Find the substrate concentration where the reaction velocity is half of \(V_{max}\). - **Calculate \(K_{cat}\):** Use the formula \(K_{cat} = \frac{V_{max}}{[E_t]}\), where \([E_t]\) is the total enzyme concentration. - **Determine Efficiency:** Assess the catalytic efficiency using \(K_{cat}/K_m\) and compare between the WT and mutant enzymes.
Expert Solution
steps

Step by step

Solved in 5 steps with 2 images

SEE SOLUTIONCheck out a sample Q&A here
Blurred answer
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Biochemistry
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
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…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON
SEE MORE TEXTBOOKS