How is the slope of a Lineweaver-Burke plot calculated?

Study for the ACS Biochemistry Exam. Explore flashcards and multiple choice questions with hints and explanations. Prepare to excel in your exam!

The Lineweaver-Burke plot is a double reciprocal plot used in enzyme kinetics, derived from the Michaelis-Menten equation. This plot is useful because it linearizes the hyperbolic relationship seen in the Michaelis-Menten equation, allowing for easier determination of kinetic parameters.

In this plot, the x-axis represents 1/[S] (the inverse of substrate concentration) and the y-axis represents 1/v (the inverse of reaction velocity). The Lineweaver-Burke equation can be expressed as:

1/v = (Km/Vmax)(1/[S]) + (1/Vmax)

In this linear equation, the slope is represented by the coefficient of the x-term, which is Km/Vmax. Thus, the slope of the Lineweaver-Burke plot specifically represents the ratio of the Michaelis constant (Km) to the maximum velocity (Vmax) of the enzyme reaction. This relationship illustrates how the substrate concentration affects the reaction velocity, particularly in cases where enzyme efficiency and saturation are factors to consider.

Understanding that the slope delineates this particular ratio is key in biochemistry, as it provides insights into enzyme behavior and kinetics, which can have significant implications in both basic research and applied fields such as drug

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