Substrate inhibition is one of the aspects of substrate specificity in vertebrate and invertebrate cholinesterases

An analytical review is performed of the literature data on the hydrolysis rate, "affinity" of substrate to active center, and constants of the "substrate inhibition" (K-SS) at hydrolysis of the choline (acetyl-, propyonyl-, butyrylcholine, acetyl-beta-methylcholine) and/or of corresponding thiocholine substrates by 59 cholinesterases from 49 different animals (chordate, insects, molluscs, nematodes). The characteristic peculiarities of enzymes from different groups of animals are revealed. The absence of regular changes of parameters of the cholinesterase substrate specificity in the course of evolutionary development is shown.