If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
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
If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
![### Educational Content: Michaelis-Menten Plot Analysis
**Figure Description:**
This figure represents a Michaelis-Menten plot demonstrating enzyme kinetics. The plot is generated using a Km (Michaelis constant) value of 0.05 mM and a Vmax (maximum reaction velocity) value of 0.309407.
**Data Table Explanation:**
The table includes columns labeled as follows:
- **[Enz]**: Concentration of enzyme, with values: 0.1, 0.15, 0.2, 0.25, 0.3.
- **Vo (Initial Velocity)**: Different initial velocities corresponding to enzyme concentrations: 0.05, 0.06, 0.07, 0.09, 0.11, 0.13, 0.16.
- **Calc Vo (Calculated Vo)**: Computed Vo values: 0.037997, 0.071402, 0.090494.
- **C (Substrate Concentration)** and **deltaVz**: Further details of substrate concentration and delta Vz calculations not fully visible.
Key constant values used in the calculations:
- **Km**: 0.05
- **Vmax**: 0.309407
**Graph Details:**
The graph plots the initial velocity (Vo) against enzyme concentration. It includes:
- **Data Points**: Represented by blue diamonds, indicating experimental measurements of initial velocity at various enzyme concentrations.
- **Curve**: A red line that demonstrates the calculated Vo values based on the Michaelis-Menten equation.
**Instructions:**
The text instructs users that the Vmax value of 0.309407 should not be changed. Anyone replicating or analyzing this data should ensure their worksheet and graph resemble the figure shown.
This plot is useful for understanding how the enzyme velocity changes concerning its concentration, allowing for insights into enzyme efficiency and substrate affinity. By analyzing the curve, one can determine how close the experimental data fits the theoretical model.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F5ef5f725-b08b-4f71-a80c-f37e47d07785%2Feba3069c-949d-4e1f-9f9c-4afcc6a2997e%2Fb7nrtc_processed.jpeg&w=3840&q=75)
Transcribed Image Text:### Educational Content: Michaelis-Menten Plot Analysis
**Figure Description:**
This figure represents a Michaelis-Menten plot demonstrating enzyme kinetics. The plot is generated using a Km (Michaelis constant) value of 0.05 mM and a Vmax (maximum reaction velocity) value of 0.309407.
**Data Table Explanation:**
The table includes columns labeled as follows:
- **[Enz]**: Concentration of enzyme, with values: 0.1, 0.15, 0.2, 0.25, 0.3.
- **Vo (Initial Velocity)**: Different initial velocities corresponding to enzyme concentrations: 0.05, 0.06, 0.07, 0.09, 0.11, 0.13, 0.16.
- **Calc Vo (Calculated Vo)**: Computed Vo values: 0.037997, 0.071402, 0.090494.
- **C (Substrate Concentration)** and **deltaVz**: Further details of substrate concentration and delta Vz calculations not fully visible.
Key constant values used in the calculations:
- **Km**: 0.05
- **Vmax**: 0.309407
**Graph Details:**
The graph plots the initial velocity (Vo) against enzyme concentration. It includes:
- **Data Points**: Represented by blue diamonds, indicating experimental measurements of initial velocity at various enzyme concentrations.
- **Curve**: A red line that demonstrates the calculated Vo values based on the Michaelis-Menten equation.
**Instructions:**
The text instructs users that the Vmax value of 0.309407 should not be changed. Anyone replicating or analyzing this data should ensure their worksheet and graph resemble the figure shown.
This plot is useful for understanding how the enzyme velocity changes concerning its concentration, allowing for insights into enzyme efficiency and substrate affinity. By analyzing the curve, one can determine how close the experimental data fits the theoretical model.
Expert Solution

This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
Step by step
Solved in 2 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