Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function.  Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.

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Chapter5: Abbreviations And Systems Of Measurement
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Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function.  Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.  

**PFK-1 Protein Analysis**

| PFK-1 protein | Vmax | Km fructose 6-phosphate | KI ATP | KI citrate |
|---------------|------|------------------------|--------|-----------|
| Wild type     | 59.27 | 0.83mM                 | 0.96   | 0.4       |
| R48C          | 58.19 | 0.84mM                 | 1.19   | >4        |
| N426S         | 67.41 | 0.82mM                 | >3     | 0.31      |
| D546N         | 30.6  | 2.04mM                 | 0.68   | 1.4       |

**Explanation:**

The table provides data derived from enzyme assays depicted in the associated graphs. Different colors and symbols indicate various PFK-1 protein variants:

- **Red squares** represent the R48C variant.
- **Blue upright triangles** indicate N426S.
- **Green upside-down triangles** signify D546N.
- **Black circles** depict wild type PFK-1.

These assays involve fructose 6-phosphate and ATP as substrates in all the experiments.

**Graph Descriptions:**

- **Graph D:** Measures the velocity of PFK-1 with varying citrate concentrations.
- **Graph E:** Assesses the velocity of PFK-1 in relation to changing ATP concentrations.
- **Graph F:** Evaluates the velocity of PFK-1 concerning different F6P concentrations.
Transcribed Image Text:**PFK-1 Protein Analysis** | PFK-1 protein | Vmax | Km fructose 6-phosphate | KI ATP | KI citrate | |---------------|------|------------------------|--------|-----------| | Wild type | 59.27 | 0.83mM | 0.96 | 0.4 | | R48C | 58.19 | 0.84mM | 1.19 | >4 | | N426S | 67.41 | 0.82mM | >3 | 0.31 | | D546N | 30.6 | 2.04mM | 0.68 | 1.4 | **Explanation:** The table provides data derived from enzyme assays depicted in the associated graphs. Different colors and symbols indicate various PFK-1 protein variants: - **Red squares** represent the R48C variant. - **Blue upright triangles** indicate N426S. - **Green upside-down triangles** signify D546N. - **Black circles** depict wild type PFK-1. These assays involve fructose 6-phosphate and ATP as substrates in all the experiments. **Graph Descriptions:** - **Graph D:** Measures the velocity of PFK-1 with varying citrate concentrations. - **Graph E:** Assesses the velocity of PFK-1 in relation to changing ATP concentrations. - **Graph F:** Evaluates the velocity of PFK-1 concerning different F6P concentrations.
The image features three graphs labeled d, e, and f, each depicting the relationship between a specific substrate concentration and relative velocity in enzymatic reactions. Here is a detailed explanation of each graph:

**Graph d: [Citrate] (mM) vs. Relative Velocity (v/V)**
- **X-Axis:** Concentration of Citrate (mM)
- **Y-Axis:** Relative velocity (v/V)
  
This graph shows the effect of citrate concentration on the relative velocity. As citrate concentration increases from 0 to 4 mM, the relative velocity decreases, as indicated by the black, blue, and green data points. The red data points indicate a constant relative velocity regardless of citrate concentration.

**Graph e: [ATP] (mM) vs. Relative Velocity (v/V)**
- **X-Axis:** Concentration of ATP (mM)
- **Y-Axis:** Relative velocity (v/V)

This graph illustrates how varying ATP concentrations affect the relative velocity of the reaction. Initially, the relative velocity increases, reaching a peak, and then decreases as ATP concentration rises from 0 to 3 mM, as demonstrated by the black, blue, green, and red data points.

**Graph f: [F6P] (mM) vs. Relative Velocity (v/V)**
- **X-Axis:** Concentration of F6P (mM)
- **Y-Axis:** Relative velocity (v/V)

The graph depicts a sigmoidal curve, showing the impact of fructose-6-phosphate (F6P) on the relative velocity. As F6P concentration increases from 0 to 4 mM, relative velocity gradually rises, approaching a maximum, as suggested by the black, blue, green, and red data points.

Each graph includes error bars representing the variability or uncertainty in the measurements. The data points are color-coded to differentiate multiple datasets or experimental conditions.
Transcribed Image Text:The image features three graphs labeled d, e, and f, each depicting the relationship between a specific substrate concentration and relative velocity in enzymatic reactions. Here is a detailed explanation of each graph: **Graph d: [Citrate] (mM) vs. Relative Velocity (v/V)** - **X-Axis:** Concentration of Citrate (mM) - **Y-Axis:** Relative velocity (v/V) This graph shows the effect of citrate concentration on the relative velocity. As citrate concentration increases from 0 to 4 mM, the relative velocity decreases, as indicated by the black, blue, and green data points. The red data points indicate a constant relative velocity regardless of citrate concentration. **Graph e: [ATP] (mM) vs. Relative Velocity (v/V)** - **X-Axis:** Concentration of ATP (mM) - **Y-Axis:** Relative velocity (v/V) This graph illustrates how varying ATP concentrations affect the relative velocity of the reaction. Initially, the relative velocity increases, reaching a peak, and then decreases as ATP concentration rises from 0 to 3 mM, as demonstrated by the black, blue, green, and red data points. **Graph f: [F6P] (mM) vs. Relative Velocity (v/V)** - **X-Axis:** Concentration of F6P (mM) - **Y-Axis:** Relative velocity (v/V) The graph depicts a sigmoidal curve, showing the impact of fructose-6-phosphate (F6P) on the relative velocity. As F6P concentration increases from 0 to 4 mM, relative velocity gradually rises, approaching a maximum, as suggested by the black, blue, green, and red data points. Each graph includes error bars representing the variability or uncertainty in the measurements. The data points are color-coded to differentiate multiple datasets or experimental conditions.
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