A C -1/a K 1-a' Wen a'Nmax (a-1) Var 1/v₂ 1/5) Slope - akma (1) a=1+- am 1 (no inhibitor) Increasing [4] 2.0 a' 1.5, a 1.5 a = 1.25 aa'1 [no inhibitor) Slope KVmax (1) a=1+ K₂ [1] a' - 1 X₁ 1/45) B O -a'/KM 1.4 1.24 1- 0.8- 0.64 024 04 -0.1 1/V -1/K m(app) a'Nmax a' = 2 a' = Slop O Control inhibitor 1/V 01 1/[S] per mM
A C -1/a K 1-a' Wen a'Nmax (a-1) Var 1/v₂ 1/5) Slope - akma (1) a=1+- am 1 (no inhibitor) Increasing [4] 2.0 a' 1.5, a 1.5 a = 1.25 aa'1 [no inhibitor) Slope KVmax (1) a=1+ K₂ [1] a' - 1 X₁ 1/45) B O -a'/KM 1.4 1.24 1- 0.8- 0.64 024 04 -0.1 1/V -1/K m(app) a'Nmax a' = 2 a' = Slop O Control inhibitor 1/V 01 1/[S] per mM
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
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![# Understanding Lineweaver-Burk Plots
The provided figure contains four Lineweaver-Burk plots (Panels A-D) that are used for studying enzyme kinetics in the presence and absence of inhibitors. These plots, which are double-reciprocal plots of the Michaelis-Menten equation, represent the relationship between 1/[S] (the reciprocal of substrate concentration) and 1/V (the reciprocal of the reaction velocity).
### Panel A:
- **Description**: Lineweaver-Burk plot demonstrating the effect of different inhibitor concentrations ([I]) on enzyme activity.
- **Key Features**:
- The x-axis represents \(1/[S]\) and the y-axis represents \(1/V\).
- Multiple lines are shown indicating different inhibitor concentrations with increasing [I] represented by higher values of α (e.g., α = 1 (no inhibitor), α = 2, α = 4).
- The lines intersect at the same point on the x-axis (which is \(−1/αK_m\)). The slope of each line increases with increasing α, indicating an increase in \(α K_m / V_{max}\).
### Panel B:
- **Description**: Lineweaver-Burk plot illustrating the competitive inhibition of an enzyme.
- **Key Features**:
- This plot shows lines with different slopes, indicating varying concentrations of a competitive inhibitor.
- The intercepts on the y-axis remain the same (1/V_max), while the intercepts on the x-axis shift, reflecting changes in \(K_m\) in the presence of different inhibitor concentrations (α' = 1, α' = 1.5, α' = 2).
### Panel C:
- **Description**: Another example of a Lineweaver-Burk plot with varying inhibitor concentrations, showing detailed mathematical relationships.
- **Key Features**:
- This plot is similar to Panel A but includes more detailed mathematical notation to illustrate how [I] influences the slope and intercepts.
- The lines are annotated with mathematical expressions indicating the relationship: \(Slope = αK_m / V_{max}\) where α is related to inhibitor concentration.
- The increase in [I] leads to changes in the slope and the x-intercept positions.
### Panel D:
- **Description**: Lineweaver-Burk plot comparing enzyme activity in the presence and absence of an inhibitor.
- **Key Features**:
- This](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F07b00a25-4bbc-4603-8563-821c16d74641%2F3224b076-39c3-4ffe-aaca-e3147f5295a8%2F2p55ra_processed.jpeg&w=3840&q=75)
Transcribed Image Text:# Understanding Lineweaver-Burk Plots
The provided figure contains four Lineweaver-Burk plots (Panels A-D) that are used for studying enzyme kinetics in the presence and absence of inhibitors. These plots, which are double-reciprocal plots of the Michaelis-Menten equation, represent the relationship between 1/[S] (the reciprocal of substrate concentration) and 1/V (the reciprocal of the reaction velocity).
### Panel A:
- **Description**: Lineweaver-Burk plot demonstrating the effect of different inhibitor concentrations ([I]) on enzyme activity.
- **Key Features**:
- The x-axis represents \(1/[S]\) and the y-axis represents \(1/V\).
- Multiple lines are shown indicating different inhibitor concentrations with increasing [I] represented by higher values of α (e.g., α = 1 (no inhibitor), α = 2, α = 4).
- The lines intersect at the same point on the x-axis (which is \(−1/αK_m\)). The slope of each line increases with increasing α, indicating an increase in \(α K_m / V_{max}\).
### Panel B:
- **Description**: Lineweaver-Burk plot illustrating the competitive inhibition of an enzyme.
- **Key Features**:
- This plot shows lines with different slopes, indicating varying concentrations of a competitive inhibitor.
- The intercepts on the y-axis remain the same (1/V_max), while the intercepts on the x-axis shift, reflecting changes in \(K_m\) in the presence of different inhibitor concentrations (α' = 1, α' = 1.5, α' = 2).
### Panel C:
- **Description**: Another example of a Lineweaver-Burk plot with varying inhibitor concentrations, showing detailed mathematical relationships.
- **Key Features**:
- This plot is similar to Panel A but includes more detailed mathematical notation to illustrate how [I] influences the slope and intercepts.
- The lines are annotated with mathematical expressions indicating the relationship: \(Slope = αK_m / V_{max}\) where α is related to inhibitor concentration.
- The increase in [I] leads to changes in the slope and the x-intercept positions.
### Panel D:
- **Description**: Lineweaver-Burk plot comparing enzyme activity in the presence and absence of an inhibitor.
- **Key Features**:
- This
![### Enzyme Activity Analysis with Lineweaver-Burk Plots - Educational Exercise
#### Question:
The Lineweaver-Burk plots in this figure represent the activities of enzymes in the absence and presence of different types of inhibitors. Which one represents the activity of the enzyme in the presence and absence of a pure noncompetitive inhibitor? (choose the one best answer).
#### Answer Choices:
- ☐ A
- ☐ B
- ☐ C
- ☐ D
#### Explanation of Graphs:
The figure of Lineweaver-Burk plots shows multiple lines, each representing enzyme activity data under different conditions. The x-axis typically represents the inverse of the substrate concentration (1/[S]), and the y-axis represents the inverse of the reaction velocity (1/V).
1. **Identifying the Correct Plot:**
- For a pure noncompetitive inhibitor, the Lineweaver-Burk plot will show lines that intersect at the same point on the x-axis, but differ in their y-intercepts. This is because a noncompetitive inhibitor does not affect the substrate binding (Km remains constant), but it decreases the maximum velocity (Vmax) of the reaction.
Make sure to carefully observe the points where the plots intersect and how they behave with the inhibitors present.
#### Notes:
- Proper understanding of how inhibitors affect enzyme kinetics is essential for interpreting these plots.
- Remember, for pure noncompetitive inhibition, the lines will meet at the x-axis but will have different slopes and y-intercepts.
Choose the most accurate answer (A, B, C, or D) based on the given explanations.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F07b00a25-4bbc-4603-8563-821c16d74641%2F3224b076-39c3-4ffe-aaca-e3147f5295a8%2F5dan4xd_processed.jpeg&w=3840&q=75)
Transcribed Image Text:### Enzyme Activity Analysis with Lineweaver-Burk Plots - Educational Exercise
#### Question:
The Lineweaver-Burk plots in this figure represent the activities of enzymes in the absence and presence of different types of inhibitors. Which one represents the activity of the enzyme in the presence and absence of a pure noncompetitive inhibitor? (choose the one best answer).
#### Answer Choices:
- ☐ A
- ☐ B
- ☐ C
- ☐ D
#### Explanation of Graphs:
The figure of Lineweaver-Burk plots shows multiple lines, each representing enzyme activity data under different conditions. The x-axis typically represents the inverse of the substrate concentration (1/[S]), and the y-axis represents the inverse of the reaction velocity (1/V).
1. **Identifying the Correct Plot:**
- For a pure noncompetitive inhibitor, the Lineweaver-Burk plot will show lines that intersect at the same point on the x-axis, but differ in their y-intercepts. This is because a noncompetitive inhibitor does not affect the substrate binding (Km remains constant), but it decreases the maximum velocity (Vmax) of the reaction.
Make sure to carefully observe the points where the plots intersect and how they behave with the inhibitors present.
#### Notes:
- Proper understanding of how inhibitors affect enzyme kinetics is essential for interpreting these plots.
- Remember, for pure noncompetitive inhibition, the lines will meet at the x-axis but will have different slopes and y-intercepts.
Choose the most accurate answer (A, B, C, or D) based on the given explanations.
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