Active site kinetics of horse serum cholinesterase.

Horse serum Cholinesterase hydrolyzes choline and p-nitrophenol esters at different rates. Deacylation and acylation seem to be the rate-limiting step for charged and uncharged substrates respectively. Activation energy is similar for the acetic, propionic, and butyric esters of thiocholine, but it is higher for p-nitrophenylpropionate. Inhibition by the tetramethyl-ammonium ion is competitive. Tetraethyl-, tetrapropyl-, and tetrabutyl-ammonium ions are mixed-type inhibitors. The pH studies demonstrated the existence of a residue, pK = 6.33, involved in catalysis.