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.
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
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.

![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.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Facf7f7d4-0a2e-4492-8754-e1a4249f75ff%2Fbed6890a-64ab-4a7c-ae8c-cbd2a8dd3f59%2Foxlah8p_processed.png&w=3840&q=75)
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