What is the impact of new km value 0.1mM compared to previous km value 0.05mM on affinity of the enzyme for substrate?

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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What is the impact of new km value 0.1mM compared to previous km value 0.05mM on affinity of the enzyme for substrate?
**Fig. 9: Michaelis-Menten Plot Explanation**

In this section, we explore a Michaelis-Menten plot generated using a value of 0.1 mM for \( K_m \).

### Observations:

1. **Data Recalculation**: A new set of calculated values is displayed in column C of the spreadsheet. These values stem from a new \( K_m \) value.
   
2. **Generated New Best-Fit**: By utilizing these recalculated data points, a new best-fit Michaelis-Menten curve (in red) is created on the graph.

### Graph/Diagram Details:

- **Data Table**: Contains numerical values used to plot the graph, showing substrate concentrations and corresponding reaction velocities.
  
- **Graph**: 
  - **Axes**: Depicts reaction velocity (V) on the Y-axis and substrate concentration ([S]) on the X-axis.
  - **Data Points**: Blue dots represent the individual data points plotted from the table values.
  - **Red Curve**: Illustrates the Michaelis-Menten fit generated from the new data. This curve demonstrates how well the data align with the expected enzyme kinetics model.

### Conclusion:

The newly adjusted data and the corresponding graph provide insights into enzyme-catalyzed reactions under different conditions. The red curve fit signifies improved alignment with theoretical predictions, showcasing the powerful application of the Michaelis-Menten equation in enzymology.
Transcribed Image Text:**Fig. 9: Michaelis-Menten Plot Explanation** In this section, we explore a Michaelis-Menten plot generated using a value of 0.1 mM for \( K_m \). ### Observations: 1. **Data Recalculation**: A new set of calculated values is displayed in column C of the spreadsheet. These values stem from a new \( K_m \) value. 2. **Generated New Best-Fit**: By utilizing these recalculated data points, a new best-fit Michaelis-Menten curve (in red) is created on the graph. ### Graph/Diagram Details: - **Data Table**: Contains numerical values used to plot the graph, showing substrate concentrations and corresponding reaction velocities. - **Graph**: - **Axes**: Depicts reaction velocity (V) on the Y-axis and substrate concentration ([S]) on the X-axis. - **Data Points**: Blue dots represent the individual data points plotted from the table values. - **Red Curve**: Illustrates the Michaelis-Menten fit generated from the new data. This curve demonstrates how well the data align with the expected enzyme kinetics model. ### Conclusion: The newly adjusted data and the corresponding graph provide insights into enzyme-catalyzed reactions under different conditions. The red curve fit signifies improved alignment with theoretical predictions, showcasing the powerful application of the Michaelis-Menten equation in enzymology.
**Figure 8: Michaelis-Menten Plot Using a K<sub>m</sub> Value of 0.05 mM**

The table and graph illustrate the Michaelis-Menten kinetics for enzymatic activity using ethanol as the substrate. The worksheet appears to be a spreadsheet, with columns labeled A through F. Below is a detailed transcription of the content:

### Table Data:

- **Column A:** (Rows 2 to 11)
  - Header: Blank
  - Ethanol concentrations from 0 to 0.5

- **Column B: Ethanol (mM)**
  - Values: 0.007, 0.016, 0.031, 0.063, 0.125, 0.25, 0.5

- **Column C: Vo (Initial velocity)**
  - Values: 0.05, 0.1, 0.2, 0.41, 0.86, 1.5, 2.0

- **Column D: Km (Michaelis constant)**
  - Value in row 13: 0.05
  - Vmax (Maximum velocity) in row 14: 0.39

- **Column E: Calc. Vo (Calculated Vo)**
  - Values: 0.006956, 0.01325, 0.025126, 0.047619, 0.086956, 0.135922, 0.19608

- **Column F: Delta V^2**
  - Values: 0.000584, 0.00129, 0.003961, 0.007749

### Graph Description:

The graph is a scatter plot with a trend line, representing the relationship between substrate concentration and reaction velocity.

- **X-Axis:** Ethanol concentration (mM)
- **Y-Axis:** Reaction velocity (Vo)

**Data Series:**
- **Blue Dots:** Experimental initial velocities (Vo) corresponding to ethanol concentrations.
- **Red Line:** Calculated initial velocities (Calc. Vo) as per the Michaelis-Menten equation.

The plot shows how reaction velocity changes with substrate concentration, demonstrating typical saturation kinetics as described by the Michaelis-Menten model.
Transcribed Image Text:**Figure 8: Michaelis-Menten Plot Using a K<sub>m</sub> Value of 0.05 mM** The table and graph illustrate the Michaelis-Menten kinetics for enzymatic activity using ethanol as the substrate. The worksheet appears to be a spreadsheet, with columns labeled A through F. Below is a detailed transcription of the content: ### Table Data: - **Column A:** (Rows 2 to 11) - Header: Blank - Ethanol concentrations from 0 to 0.5 - **Column B: Ethanol (mM)** - Values: 0.007, 0.016, 0.031, 0.063, 0.125, 0.25, 0.5 - **Column C: Vo (Initial velocity)** - Values: 0.05, 0.1, 0.2, 0.41, 0.86, 1.5, 2.0 - **Column D: Km (Michaelis constant)** - Value in row 13: 0.05 - Vmax (Maximum velocity) in row 14: 0.39 - **Column E: Calc. Vo (Calculated Vo)** - Values: 0.006956, 0.01325, 0.025126, 0.047619, 0.086956, 0.135922, 0.19608 - **Column F: Delta V^2** - Values: 0.000584, 0.00129, 0.003961, 0.007749 ### Graph Description: The graph is a scatter plot with a trend line, representing the relationship between substrate concentration and reaction velocity. - **X-Axis:** Ethanol concentration (mM) - **Y-Axis:** Reaction velocity (Vo) **Data Series:** - **Blue Dots:** Experimental initial velocities (Vo) corresponding to ethanol concentrations. - **Red Line:** Calculated initial velocities (Calc. Vo) as per the Michaelis-Menten equation. The plot shows how reaction velocity changes with substrate concentration, demonstrating typical saturation kinetics as described by the Michaelis-Menten model.
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