In biochemistry, an Eadie-Hofstee diagram (also Woolf-Eadie-Augustinsson-Hofstee or Eadie-Augustinsson plot) is a graphical representation of enzyme kinetics in which reaction velocity is plotted as a function or the velocity vs. substrate concentration ratio:
![v = -K_m { v \over [S] } + v_{max}](a/../upload/math/ac8d93c9d0c6e0a446aab137dd3cc97a.png)
where v represents reaction velocity, Km is the Michaelis-Menten constant, [S] is the substrate concentration, and vmax is the maximum reaction velocity.
Like other techniques that linearize the Michaelis-Menten equation, the Eadie-Hofstee plot allows for rapid identification of important kinetic terms like Km and vmax. It is also more robust against error-prone data than the Lineweaver-Burke plot, particularly because it gives equal weight to data points in any range of substrate concentration or reaction velocity. (The Lineweaver-Burke plot unevenly weights such points.)
One drawback from the Eadie-Hofstee approach is that neither ordinate or abscissa represent independent variables: both are dependent on reaction velocity. Thus any experimental error will be present in both axes.