Answer / maneravindrag

he plot provides a useful graphical method for analysis of
the Michaelis–Menten equation:


Taking the reciprocal gives


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

use: The Lineweaver–Burk plot was widely used to
determine important terms in enzyme kinetics, such as Km and
Vmax, before the wide availability of powerful computers and
non-linear regression software. As the y-intercept of such a
graph is equivalent to the inverse of Vmax; the x-intercept
of the graph represents −1/Km. It also gives a quick, visual
impression of the different forms of enzyme inhibition.
The double reciprocal plot distorts the error structure of
the data, and it is therefore unreliable for the
determination of enzyme kinetic parameters. Although it is
still used for representation of kinetic data,[2] non-linear
regression or alternative linear forms of the Michaelis–
Menten equation such as the Hanes-Woolf plot or Eadie–
Hofstee plot are generally used for the calculation of
parameters.[3]
When used for determining the type of enzyme inhibition, the
Lineweaver–Burk plot can distinguish competitive, non-
competitive and uncompetitive inhibitors. Competitive
inhibitors have the same y-intercept as uninhibited enzyme
(since Vmax is unaffected by competitive inhibitors the
inverse of Vmax also doesn't change) but there are different
slopes and x-intercepts between the two data sets. Non-
competitive inhibition produces plots with the same x-
intercept as uninhibited enzyme (Km is unaffected) but
different slopes and y-intercepts. Uncompetitive inhibition
causes different intercepts on both the y- and x-axes but
the same slope

problem:The Lineweaver–Burk plot is classically used in
older texts, but is prone to error, as the y-axis takes the
reciprocal of the rate of reaction – in turn increasing any
small errors in measurement. Also, most points on the plot
are found far to the right of the y-axis (due to limiting
solubility not allowing for large values of [S] and hence no
small values for 1/[S]), calling for a large extrapolation
back to obtain x- and y-intercepts.

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