Abstract
Data on the kinetics of the hydrolysis of various carboxylic acid esters by two main types of cholinesterases – acetylcholinesterase from human erythrocytes and butyrylcholinesterase from horse blood serum – are surveyed. It is shown that the rate of enzyme hydrolysis depends significantly on the structure of the acyl part of the ester molecule, the nature of the ester heteroatom, the structure of the alcohol component, and particularly the structure of the onium group. Esters based on natural products are of special interest as specific substrates of these enzymes. The role of the productive and non-productive sorption of the substrates in enzyme catalysis is demonstrated.
The bibliography includes 81 references.