The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025 mL of an enzyme sample that is 4.0 µg/mL and determined that the following Vmax = 2.442 x 102umoles/min What is the turnover number of this enzyme (in units of #/sec)?
The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025 mL of an enzyme sample that is 4.0 µg/mL and determined that the following Vmax = 2.442 x 102umoles/min What is the turnover number of this enzyme (in units of #/sec)?
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
Related questions
Question
![---
## Enzyme Kinetics: Understanding Turnover Number
The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa) and features an identical active site on each of its four subunits. To study this enzyme, we performed a series of enzyme kinetic experiments with an enzyme sample concentration of 4.0 µg/mL. From these experiments, we determined a Vmax (maximum reaction velocity) of 2.442 x 10^-2 µmoles/min.
### Problem Statement
**Question:** What is the turnover number of this enzyme (in units of #/sec)?
**Options:**
- 76/sec
- 305/sec
- 152/sec
- 4579/sec
- 1526/sec
### Explanation
The turnover number (also called kcat) is a measure of the catalytic activity of an enzyme. It is defined as the number of substrate molecules converted into product by an enzyme molecule in a unit of time when the enzyme is fully saturated with substrate.
### Calculation of the Turnover Number
1. **Determine enzyme concentration in moles:**
\[
\text{Enzyme concentration} = \frac{4.0 \, \text{µg/mL}}{150,000 \, \text{g/mol}} = \frac{4.0 \times 10^{-6} \, \text{g/mL}}{150,000 \, \text{g/mol}} = 2.67 \times 10^{-11} \, \text{mol/mL}
\]
2. **Convert moles to per minute Vmax:**
\[
Vmax = 2.442 \times 10^{-2} \, \mu \text{moles/min}
\]
3. **Convert Vmax from per minute to per second:**
\[
Vmax = \frac{2.442 \times 10^{-2} \, \mu \text{moles/min}}{60 \, \text{sec/min}} = 4.07 \times 10^{-4} \, \mu \text{moles/sec}
\]
4. **Calculate kcat:**
\[
kcat = \frac{Vmax}{[\text{enzyme concentration}]}
\]
Since there are 4 active sites](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F98834d82-84c5-4d71-9bf6-a3211e165794%2F2f44e712-0ff2-40bf-b563-883b38411118%2F37hj1n_processed.jpeg&w=3840&q=75)
Transcribed Image Text:---
## Enzyme Kinetics: Understanding Turnover Number
The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa) and features an identical active site on each of its four subunits. To study this enzyme, we performed a series of enzyme kinetic experiments with an enzyme sample concentration of 4.0 µg/mL. From these experiments, we determined a Vmax (maximum reaction velocity) of 2.442 x 10^-2 µmoles/min.
### Problem Statement
**Question:** What is the turnover number of this enzyme (in units of #/sec)?
**Options:**
- 76/sec
- 305/sec
- 152/sec
- 4579/sec
- 1526/sec
### Explanation
The turnover number (also called kcat) is a measure of the catalytic activity of an enzyme. It is defined as the number of substrate molecules converted into product by an enzyme molecule in a unit of time when the enzyme is fully saturated with substrate.
### Calculation of the Turnover Number
1. **Determine enzyme concentration in moles:**
\[
\text{Enzyme concentration} = \frac{4.0 \, \text{µg/mL}}{150,000 \, \text{g/mol}} = \frac{4.0 \times 10^{-6} \, \text{g/mL}}{150,000 \, \text{g/mol}} = 2.67 \times 10^{-11} \, \text{mol/mL}
\]
2. **Convert moles to per minute Vmax:**
\[
Vmax = 2.442 \times 10^{-2} \, \mu \text{moles/min}
\]
3. **Convert Vmax from per minute to per second:**
\[
Vmax = \frac{2.442 \times 10^{-2} \, \mu \text{moles/min}}{60 \, \text{sec/min}} = 4.07 \times 10^{-4} \, \mu \text{moles/sec}
\]
4. **Calculate kcat:**
\[
kcat = \frac{Vmax}{[\text{enzyme concentration}]}
\]
Since there are 4 active sites
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 with 4 images

Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Recommended textbooks for you

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Organic Chemistry
Chemistry
ISBN:
9780078021558
Author:
Janice Gorzynski Smith Dr.
Publisher:
McGraw-Hill Education

Chemistry: Principles and Reactions
Chemistry
ISBN:
9781305079373
Author:
William L. Masterton, Cecile N. Hurley
Publisher:
Cengage Learning

Elementary Principles of Chemical Processes, Bind…
Chemistry
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY