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Introduction to Enzyme Kinetics Calculators
Below are some calculators that will help you when you need to calculate key enzyme kinetics parameters from your experimental data.
When studying biochemical reactions, such as those catalyzed by enzymes or mediated by transporters, it’s important to understand how the reaction rate (v) changes as the
substrate concentration ([S]) increases.
In many cases, the reaction rate increases almost linearly at low
[S] (first-order kinetics) and then gradually levels off as the enzyme or transporter becomes saturated, reaching a maximum rate (Vₘₐₓ).
This behavior is described by the Michaelis-Menten equation:
Where:
• Vₘₐₓ is the maximum reaction velocity, achieved when the enzyme is fully saturated with substrate.
• Kₘ is the Michaelis constant, the substrate concentration at which the reaction rate is half of Vₘₐₓ.
• [S] is the substrate concentration.
How to Use These Calculators:
- Michaelis-Menten Plot (v vs. [S]):
Use this plot to visualize the overall hyperbolic (saturation) behavior of an enzyme. It shows how the reaction rate increases with substrate concentration until it levels off at Vₘₐₓ. Enter your experimental values to see the full curve.
- Lineweaver-Burk Plot (1/v vs. 1/[S]):
This double reciprocal plot linearizes the Michaelis-Menten curve. It is useful for determining Vₘₐₓ and Kₘ through linear regression, where the slope equals Km/VmaxKₘ/VₘₐₓKm/Vmax and the y-intercept equals 1/Vmax1/Vₘₐₓ1/Vmax.
- Eadie-Hofstee Plot (v vs. v/[S]):
This plot re-arranges the Michaelis-Menten equation into a linear form, where the y-intercept gives Vₘₐₓ and the negative slope represents Kₘ. It offers an alternative way to evaluate your kinetic parameters and can help identify experimental errors.
- Hanes-Woolf Plot ([S]/v vs. [S]):
In this plot, the y-axis is [S]/v[S]/v[S]/v and the x-axis is. The slope equals 1/Vmax1/Vₘₐₓ1/Vmax and the y-intercept equals Km/VmaxKₘ/VₘₐₓKm/Vmax. This method is often considered more robust against errors in experimental measurements.
