Editing Lineweaver–Burk plot (section)

=== Mixed inhibition ===
Pure noncompetitive inhibition is rare, and mixed inhibition is much more common. In mixed inhibition the apparent value of <math>V</math> is decreased, and that of <math>K_\mathrm{m}</math> is changed—usually increased, meaning that the affinity usually decreases with mixed inhibition.

Cleland recognized that pure noncompetitive inhibition was very rare in practice, occurring mainly with effects of protons and some metal ions, and he redefined ''noncompetitive'' to mean ''mixed''.<ref>{{cite journal | doi= 10.1016/0926-6569(63)90226-8 | journal =Biochim. Biophys. Acta  | volume = 67 | number = 2 | pages = 173–187 | title = The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theory | author = Cleland, W. W.}}</ref> Many authors have followed him in this respect, but not all.