Two types of reversible inhibition are:
This inhibitor binds to the same site as the substrate. It therefore competes since both substrate and inhibitor are similar in shape.
Effect on Vmax: it is the same velocity in the presence of competitive inhibitors.
Effect on Km: the Michaelis constant increases in the presence of competitive inhibitors.
Occurs when the inhibitor binds to a free enzyme or enzyme substrate complex preventing the substrate from binding to its active site.
Effect on Vmax: it decreases in the presence of noncompetitve inhibitors.
Effect on Km: the Michaelis constant is unchanged in the presence of noncompetitive inhibitors.
Graph 1 showing Michaelis – Menten curves for competitve and noncompetive inhibition:
Graph 2 showing Lineweaver – Burk plots for competitve and noncompetive inhibition: