Cholinesterase(redirected from Cholinesterases)
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Related to Cholinesterases: true cholinesterase
any of a group of enzymes of the hydrolase class that act as a catalyst in the hydrolysis of choline esters, according to the equation
(CH3)3N + CH2CH2OCOR + H2O → (CH3)3N+ CH2CH2OH + RCOOH
The cholinesterase of the greatest biological importance is that of the nervous system, acetylcholinesterase (ACE), which acts as a catalyst mainly for the hydrolysis of acetylcholine (R = CH3). Cholinesterases that hydrolyze predominately the esters of choline and other carboxylic acids, such as propionic and butyric acid, have retained the trivial name cholinesterase.
ACE catalyzes the hydrolysis of acetylcholine to acetic acid and choline. Acetylcholine, a highly active substance, is secreted in the synapses of the nervous system and takes part in the transmission of nerve impulses from one nerve cell to the next and from nerve cells to the appropriate organs, such as muscles and endocrine glands. It must be rapidly broken down, however, because accumulations of it block the transmission of nerve impulses and cause paralysis—that is, the loss of nerve functions. For this reason, substances that suppress ACE activity are highly toxic; such substances include organophosphate insecticides, physostigmine, and proserine.
An enzyme with properties similar to those of ACE is found in erythrocytes, but its biological function is not yet known. Less specific cholinesterases are found in blood serum and certain organs and tissues of animals. The most active ACE has been discovered in the electric organs of fish of the suborder Batoidea. Individual cholinesterases of high purity have been obtained from various organs and tissues.
All cholinesterases are proteins with molecular weights ranging from 70,000 to 1,000,000; they contain no coenzymes of low molecular weight. A very important role in the catalytic activity of cholinesterases is played by the amino acids serine, histidine, aspartic acid, and glutamic acid.
V. A. IAKOVLEV