Why is it preferable to use a Lineweaver-Burk over a Michaelis-Menten plot when studying enzyme kinetics?

• A. To directly visualize K_m & V_max on the plot.
• B. To plot kinetic data as a hyperbolic curve instead of a line.
• C. To obtain a more accurate measure of the V₀.
• D. To remove terms that cannot be calculated in a typical enzyme kinetics experiment.
• E. To get more accurate estimates of K_m & V_max.

Answer: (E)

Verified step by step guidance

1. Understand the purpose of enzyme kinetics: Enzyme kinetics studies the rates of enzyme-catalyzed reactions, and two important parameters are Km (Michaelis constant) and Vmax (maximum reaction velocity).
2. Recognize the limitations of the Michaelis-Menten plot: The Michaelis-Menten plot is a hyperbolic curve that can make it difficult to accurately determine Km and Vmax directly from the graph, especially when experimental data is noisy or incomplete.
3. Introduce the Lineweaver-Burk plot: The Lineweaver-Burk plot is a double-reciprocal plot (1/V0 vs. 1/[S]) that linearizes the Michaelis-Menten equation, making it easier to determine Km and Vmax.
4. Explain how the Lineweaver-Burk plot works: In the Lineweaver-Burk plot, the y-intercept represents 1/Vmax, and the x-intercept represents -1/Km. This linear relationship allows for more precise estimation of these parameters.
5. Conclude with the advantage of the Lineweaver-Burk plot: By transforming the data into a linear form, the Lineweaver-Burk plot provides more accurate estimates of Km and Vmax, which is why it is often preferred over the Michaelis-Menten plot for analyzing enzyme kinetics.