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What is the Difference Between Michaelis Menten and Lineweaver Burk Plot

June 10, 2022 Posted by Madhu

The key difference between Michaelis Menten and Lineweaver Burk plot is that Michaelis Menten’s plot gives a more accurate estimate of Vmax and more accurate information about inhibition than the Lineweaver Burk plot.

Michaelis Menten and Lineweaver Burk’s plot are two important models in analytical chemistry as well as in biochemistry because they are helpful in determining enzyme kinetics.

CONTENTS

1. Overview and Key Difference
2. What is Michaelis Menten Plot
3. What is Lineweaver Burk Plot
4. Michaelis Menten vs Lineweaver Burk Plot in Tabular Form
5. Summary – Michaelis Menten vs Lineweaver Burk Plot 

What is Michaelis Menten Plot?

Michaelis Menten plot can be described as a model useful in describing the rate of enzymatic reactions. This is one of the best-known models of enzyme kinetics. The model was named after the German biochemist Leonor Michaelis and the Canadian physician Maud Menten. Michaelis Menten plot works by relating reaction rate to the concentration of a substrate.

Michaelis Menten and Lineweaver Burk Plot - Side by Side Comparison

Michaelis Menten equation can be given as follows:

V = d[P]/dt = Vmax ([S]/KM + [S])

In this equation, Vmax refers to the maximum rate achieved by the system, which happens at the saturating substrate concentration for a particular enzyme concentration. At the point where the numerical value of KM is equal to the substrate concentration, the reaction rate becomes half of Vmax.

What is Lineweaver Burk Plot?

Lineweaver Burk plot can be described as a graphical representation of the Lineweaver Burk equation of enzyme kinetics. This phenomenon was first described by Hans Lineweaver and Dean Burk in 1934. This plot is correct when the enzyme kinetics obeys ideal second-order kinetics. But non-linear regression is required for systems that are not behaving ideally. Moreover, the double reciprocal plot distorts the error structure of the data. Therefore, it is not the most accurate tool for the determination of enzyme kinetic parameters. We can use the Michaelis Menten equation in its non-linear regression or alternative linear form for the calculation of parameters.

Michaelis Menten vs Lineweaver Burk Plot in Tabular Form

We can use this type of plot for the determination of enzyme inhibition. Here, this plot helps in distinguishing competitive, non-competitive, and uncompetitive inhibitors. Using this model, we can also compare various modes of inhibition with the uninhibited reaction.

Although this plot is important in the determination of variables in enzyme kinetics, it shows errors. For example, the y-axis of the plot takes the reciprocal of the rate of reaction. This means the small errors in measurement are more noticeable here. Furthermore, the values derived from low substrate concentration are on the far right of the plot. This has a larger impact on the slope of the line; therefore, it particularly has an impact on the value of Km.

What is the Difference Between Michaelis Menten and Lineweaver Burk Plot?

Michaelis Menten plot is a model useful in describing the rate of enzymatic reactions, while Lineweaver Burk plot is a graphical representation of the Lineweaver Burk equation of enzyme kinetics. The key difference between Michaelis Menten and Lineweaver Burk plot is that Michaelis Menten’s plot is more accurate in providing information about inhibition than Lineweaver Burk plot and gives a better estimate of Vmax.

The below infographic presents the differences between Michaelis Menten and Lineweaver Burk plot in tabular form for side-by-side comparison.

Summary – Michaelis Menten vs Lineweaver Burk Plot

Michaelis Menten and Lineweaver Burk’s plot are two important models in analytical chemistry as well as in biochemistry as they help in determining enzyme kinetics. The key difference between Michaelis Menten and Lineweaver Burk plot is their accuracy. When compared to Lineweaver Burk plot, Michaelis Menten’s plot provides a more accurate estimate of Vmax and more accurate information about enzyme inhibition.

Reference:

1. “Enzyme Kinetics.” Michaelis-Menten Kinetics and Briggs-Haldane Kinetics.

Image Courtesy:

1. “Michaelis Menten curve 2” By Thomas Shafee – Own work (CC BY 4.0) via Commons Wikimedia
2. “Enzyme Inhibition lineweaver-burk plots” By Bizz1111 – Own work (CC0) via Commons Wikimedia

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Filed Under: Analytical Chemistry

About the Author: Madhu

Madhu is a graduate in Biological Sciences with BSc (Honours) Degree and currently persuing a Masters Degree in Industrial and Environmental Chemistry. With a mind rooted firmly to basic principals of chemistry and passion for ever evolving field of industrial chemistry, she is keenly interested to be a true companion for those who seek knowledge in the subject of chemistry.

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