Enzyme Kinetics
Which type of inhibition does this plot show?
Michaelis-Menten kinetics describe how reaction rate depends on substrate: v = Vmax[S] / (Km + [S]). Vmax is the rate at saturation, and Km is the substrate concentration at half of Vmax, so a lower Km means tighter substrate binding.
Three modes: Read the plot (name the inhibition type from a Lineweaver-Burk graph), Predict the effect (on Km and Vmax), and Concepts (Km, Vmax, kcat, catalytic efficiency, and more).
On a Lineweaver-Burk plot the y-intercept is 1/Vmax, the x-intercept is -1/Km, and the slope is Km/Vmax. Competitive inhibitors meet the control line on the y-axis (Vmax unchanged), noncompetitive inhibitors meet it on the x-axis (Km unchanged), and uncompetitive inhibitors run parallel to it (both fall together).