The simplest equation for the rate  of an enzyme-catalysed reaction as a function of the substrate concentration  is the Michaelis-Menten equation, which can be written as follows:
in which  is the rate at substrate saturation (when  approaches infinity, or limiting rate, and  is the value of  at half-saturation, i.e. for , known as the Michaelis constant. Eadie and Hofstee independently transformed this into straight-line relationships, as follows: Taking reciprocals of both sides of the equation gives the equation underlying the Lineweaver–Burk plot: 
: &middot; 
This can be rearranged to express a different straight-line relationship:
: &middot; 
which shows that a plot of  against  is a straight line with intercept  on the ordinate, and slope  (Hofstee plot). In the Eadie plot the axes are reversed, but the principle is the same. These plots are kinetic versions of the Scatchard plot used in ligand-binding experiments.