Lineweaver–Burk plot

Because  V_max is accomplished  at in?nite  substrate  concentration,  it is not possible  to estimate  V_max  (and  therefore  K_m)  from  a  hyperbolic   plot  as  described  in  Figure. Moreover, Vmax   and Km   can be determined experimentally through measuring V₀ at

Figure: The relationship between substrate concentration [S] and initial reaction velocity (V₀ ). (a) A direct plot, (b) a Lineweaver-Burk double-reciprocal plot

various substrate concentrations see in the figure. Then a double reciprocal or Lineweaver–Burk plot of 1/V₀ against 1/[S] is made that plot is a derivation of the Michaelis–Menten equation which is:

that gives a single straight line with the intercept on the y-axis equal to 1/V_max and the  intercept  on  the  x-axis  equal  to 1/K_m.  The slope of the line is equivalent to K_m/V_max.  The Lineweaver–Burk plot is also a useful way of determining how an inhibitor binds to an enzyme. The Km and Vmax can also be determined from an Eadie-Hofstee plot of V₀/[S] beside V₀ whereas the intercept on the x-axis equals V_max and the slope of the line is equal to1/Km.

Although the Michaelis–Menten model gives a very good model of the experimental data for several enzymes, a few enzymes do not conform to Michaelis–Menten kinetics. These enzymes like as ATCase or aspartate transcarbamoylase are known as allosteric enzymes.