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
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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.
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.
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