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What does Vmax represent in the context of enzyme kinetics?
How does increasing substrate concentration ([S]) affect the Vmax of an enzyme-catalyzed reaction?
The Michaelis-Menten equation is used to describe the kinetics of enzyme-catalyzed reactions. What does the Michaelis constant (Km) represent in this model?
Refer to the following experimental data obtained from an enzyme kinetics study:
Substrate Concentration [S] (mM) | Initial Reaction Rate V0 (μmol/min) |
---|---|
1.0 | 15 |
2.5 | 25 |
5.0 | 35 |
7.5 | 40 |
10.0 | 45 |
12.5 | 48 |
15.0 | 50 |
20.0 | 50 |
Based on this data, what is the approximate Vmax for this enzyme-catalyzed reaction?
In an experiment to determine the Michaelis constant () for a specific enzyme, the initial reaction rates () were measured at various substrate concentrations (). The following table presents the collected data:
Substrate Concentration [S] (mM)
|
Initial Reaction Rate V0 (μmol/min) |
---|---|
1.0 | 15 |
2.5 | 25 |
5.0 | 35 |
7.5 | 40 |
10.0 | 45 |
12.5 | 48 |
15.0 | 50 |
20.0 | 50 |
Given the data, what is the approximate value of the enzyme for this substrate?