Linear forms of michaelis-menten equation

 The Michaelis-Menten equation describes the rate of enzymatic reactions by relating reaction rate 

v to substrate concentration [S], maximum reaction rate Vmax, and the Michaelis constant Km. The equation is given by:

v=Vmax[S]Km+[S]

To determine Km and Vmax, the Michaelis-Menten equation can be linearized in a few different ways. The two most common linear forms are the Lineweaver-Burk plot and the Eadie-Hofstee plot.


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Lineweaver-Burk Plot (Double Reciprocal Plot)

The Lineweaver-Burk plot is obtained by taking the reciprocal of both sides of the Michaelis-Menten equation:

1v=Km+[S]Vmax[S]

This can be rearranged to:

1v=KmVmax1[S]+1Vmax

This equation is in the form of a straight line y=mx+b where:

  • y=1v
  • x=1[S]
  • Slope m=KmVmax
  • Y-intercept b=1Vmax

By plotting 1v against 1[S]Vmax can be determined from the y-intercept (which is 1Vmax) and Km can be determined from the slope (which is KmVmax).

Eadie-Hofstee Plot

The Eadie-Hofstee plot is obtained by rearranging the Michaelis-Menten equation to express v as a function of v[S]:

v=VmaxKm(v[S])

This is also in the form of a straight line y=mx+b where:

  • y=v
  • x=v[S]
  • Slope m=Km
  • Y-intercept b=Vmax

By plotting v against v[S]Vmax can be determined from the y-intercept and Km can be determined from the negative slope.

Summary

  1. Lineweaver-Burk Plot1v=KmVmax1[S]+1Vmax

    • Plot 1v vs. 1[S]
    • Slope = KmVmax
    • Y-intercept = 1Vmax
  2. Eadie-Hofstee Plotv=VmaxKm(v[S])

    • Plot v vs. v[S]
    • Slope = Km
    • Y-intercept = Vmax

Using these linear transformations, Km and Vmax can be determined from experimental data by fitting the appropriate straight lines and extracting the parameters from the slope and intercept.

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