Mixed inhibition refers to a combination of two different types of reversible enzyme inhibition--competitive inhibition and uncompetitive inhibition. The term 'mixed' is used when the inhibitor can bind to either the free enzyme or the enzyme-substrate complex. In mixed inhibition, the inhibitor binds to a site different from the active site where the substrate binds.

Mathematically, mixed inhibition occurs when the alpha and alpha-prime factors (introduced into the Michaelis-Menten equation to account for competitive and uncompetitive inhibition, respectively) are both present (i.e., greater than unity).

In a special case of mixed inhibition, the alpha and alpha-prime factors are equal, and noncompetitive inhibition occurs.

With this type of inhibition K_m increases and V_max decreases.