# Lineweaver–Burk Plot

the presence of an infinite amount of substrate and is therefore impossible to determine Km and Vmax from a hyperbolic graph. Due...

MN Editors

Microbiology Notes is an educational niche blog related to microbiology (bacteriology, virology, parasitology, mycology, immunology, molecular biology, biochemistry, etc.) and different branches of biology.

Lineweaver–Burk Plot

Since, Vmax is reached in the presence of an infinite amount of substrate and is therefore impossible to determine Km and Vmax from a hyperbolic graph. Due to this issue the equation of Michaelis-Menten was converted into an equation of straight lines using Lineweaver along with Burk.

The lineweaver-burk graph (or the double reciprocal plot) is a graph of the Lineweaver Burk equation of enzyme kinetics. It was first described in 1934 by Hans Lineweaver and Dean Burk in 1934. The plot is a reinterpretation from the Michaelis-Menten formula and is depicted asfollows:

## where V is the reaction velocity (the reaction rate), Km is the Michaelis–Menten constant, Vmax is the maximum reaction velocity, and [S] is the substrate concentration.

It is straight lines that has the line’s intercept on the y-axis being equal to 1Vmax and the intercept on the x-axis is equal to Km/Vmax. The line’s slope will be Km/Vmax.

Vmax and Km are determined by measuring the V0 in different concentrations of substrate. A double reciprocal or Lineweaver-Burk graph of 1/V0 and the ratio 1/[S] can be constructed.

Reversible enzyme inhibitors are classified as competitive or not, and are distinguished by an Lineweaver-Burk chart. It’s a good method to determine how inhibitors bind to an enzyme. It is possible to detect competitive inhibition through a Lineweaver-Burk graph in the event that V0 is determined at different concentrations of substrate with a predetermined amount of inhibitor.

An inhibitor that is competitive enhances that line’s slope in the Lineweaver-Burk plot. It also affects the angle on the x-axis (since Km is increased) However, it keeps the intercept on y-axis unaltered (since Vmax remains constant). Noncompetitive inhibition may also be detected on a Lineweaver Burk plot because it increases that slope of the experiment line, and alters direction of the intercept along the y-axis (since Vmax decreases) however, it does not alter the x-axis intercept unaltered (since Km is constant).

## Uses of Lineweaver–Burk Plot

• The method is used to define crucial terms in enzyme kinetics like Km and Vmax prior to the widespread access to powerful computers and non-linear regression software.
• Provides a brief, visual glimpse of the various types of inhibition of enzymes.
Need a Note? Request us
Request
0
0

Microbiology Notes is an educational niche blog related to microbiology (bacteriology, virology, parasitology, mycology, immunology, molecular biology, biochemistry, etc.) and different branches of biology.

in

in