Three mechanisms have been suggested to describe the inhibition of acetylcholinesterase (EC. 3.1.1.7) by an excess of acetylcholine. (i) Substrate inhibition occurs through the reaction of acetylcholine with acetylated enzyme. The deacetylation of this ternary complex is supposed to be completely inhibited. (ii) A ternary complex is formed as in (i). However, the deacetylation is not completely inhibited. (iii) A two-site-mechanism is discussed. Acetylcholine binds either to the active site or to the modifier site. Binding to the latter changes the activity of the active site. Steady state treatment was applied to (i)-(iii). A least squares fit led to catalytic parameters. It is demonstrated that mechanism (ii) is the most simple one which can describe satisfactorily the experimental data. Limits for a set rate constants are derived from the catalytic parameters. A numerical integration shows that the steady state approximation may be used even when the mechanisms are rather complex.