This applet demonstrates kinetics of an enzyme acting on two substrates. Click on the Start button to plot reaction velocity (V) against the concentration of substrate A ([SB]) [left hand graph panel] and to show the corresponding Eadie-Hofstee plots (V/[SB] versus V) at different fixed concentrations of substrate A [right graph panel].

Apparent V_maxs are equal to the intercepts on the V/[SB] axis divided by the negative of the slopes of the regression lines in the right graph panel. Apparent K_ms are equal to the negative of the slopes of the regression lines in the right graph panel. The curves drawn through the data points in the left graph panel are obtained by substituting apparent V_maxs and corresponding apparent K_ms in the Michaelis-Menten equation:

Colors refer to different fixed concentrations of substrate A (SA1 = 1.0 mM --- BLACK; SA2 = 0.5 mM --- RED; SA3 = 0.2 mM --- BLUE; SA4 = 0.1 mM --- GREEN; SA5 = 0.05 mM --- MAGENTA).