Non Competitive Inhibition Lineweaver Burk

Since, V_max is achieved at space substrate concentration, it is incommunicable to gauge V_max and hence K_m from a hyperbolic plot.
Because of this difficulty, the Michaelis–Menten equation was transformed into an equation for a straight line by Lineweaver and Burk.
The Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934.
This plot is a derivation of the Michaelis–Menten equation and is represented as:

where V is the reaction velocity (the reaction rate), Thousand_m is the Michaelis–Menten constant, 5_max is the maximum reaction velocity, and [South] is the substrate concentration.

It gives a straight line, with the intercept on the y-axis equal to 1/V_max, and the intercept on the x-axis equal to One thousand_chiliad/V_max. The slope of the line is equal to Yard_yard/V_max.
V_max and M_m tin can be determined experimentally by measuring Five₀at different substrate concentrations. Then a double reciprocal or Lineweaver–Burk plot of 1/V₀ against 1/[S] is made.

Reversible enzyme inhibitors can exist classified equally either competitive or noncompetitive, and can exist distinguished via a Lineweaver–Burk plot.
Information technology is a useful mode of determining how an inhibitor binds to an enzyme.
Competitive inhibition can exist recognized by using a Lineweaver–Burk plot if Five₀ is measured at different substrate concentrations in the presence of a stock-still concentration of inhibitor.
A competitive inhibitor increases the slope of the line on the Lineweaver–Burk plot, and alters the intercept on the x-axis (since Km is increased), but leaves the intercept on the y- axis unchanged (since 5_max remains constant).
Noncompetitive inhibition can besides be recognized on a Lineweaver–Burk plot since information technology increases the slope of the experimental line, and alters the intercept on the y-axis (since V_max is decreased), just leaves the intercept on the 10-axis unchanged (since Km remains constant).

Used to determine important terms in enzyme kinetics, such as K_grandand 5_max, before the wide availability of powerful computers and non-linear regression software.
Gives a quick, visual impression of the different forms of enzyme inhibition.

David Hames and Nigel Hooper (2005). Biochemistry. Third ed. Taylor & Francis Group: New York.
Smith, C. M., Marks, A. D., Lieberman, M. A., Marks, D. B., & Marks, D. B. (2005). Marks' basic medical biochemistry: A clinical approach. Philadelphia: Lippincott Williams & Wilkins.
https://en.wikipedia.org/wiki/Lineweaver%E2%80%93Burk_plot

Source: https://microbenotes.com/lineweaver-burk-plot/