Dec 1, 1980

Propionylcholinesterases from the brain of Mollusca Interaction with substrates and inhibitors

G M Grigor'eva


The kinetics of hydrolysis of choline esters under the action of propyonylcholinesterases (acylcholine--acylhydrolase, EC from the brain of some Gastropoda--Lymnaea stagnalis, Murex frunculus and Rapana thomasiana were studied. It was shown that the propyonylcholinesterases under study differ from typical cholinesterases of vertebrates. Their catalytic action is characterized by a high rate of hydrolysis of propyonylcholine (PCh) and butyrylcholine (BCh), inhibition of activity by high concentrations of the substrates and the inability to catalyze the hydrolysis of benzoyl choline and acetyl-beta-methylcholine (AMCh) with the exception of a low rate of AMCh hydrolysis induced by propyonylcholinesterase of L. stagnalis. The correlation of the hydrolysis rates of PCh, BCh and acetylcholine (ACh) is different. A comparison of the kinetic parameters of Km, V and V/Km for the enzymatic hydrolysis of substrates allowed to establish differences between various propyonylcholinesterases coupled with the values of the kinetic constants for initial and final steps of hydrolysis. Propyonylcholinesterase from M. trunculus is a "proper" propyonylcholinesterase, since PCh is the best substrate for it, both at the stage of the enzyme-...Continue Reading

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Mentioned in this Paper

Structure-Activity Relationship
Choline esters, parasympathomimetics

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