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An enzyme found in blood and in various other tissues that catalyzes hydrolysis of choline esters, including acetylcholine. Abbreviated chE.



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.


References in periodicals archive ?
2013), however these isolated alkaloids were more BChE selective.
The finding that BCHE gene variant predicts the extent of plaque deposit in PET scans among people at risk for Alzheimer's disease is likely to reinvigorate research into drugs that could modify the disease by affecting the BCHE enzyme or its metabolic pathway," he said.
Individuals with the rare silent (S) phenotype completely lack or have only minimal BChE activity (8).
The strongest inhibitory activities against BChE were observed with the essential oils of M.
Coding exons of the BCHE gene were amplified as nine independent fragments by PCR, and each amplified product was analyzed by single-stranded DNA conformation polymorphism analysis (2, 4) and denaturing HPLC (WAVE System; Transgenomic).
Key differences in the primary sequences of AChE and BChE result in active site-containing peptide fragments (Figure 5) of different sizes after trypsin and chymotrypsin digests.
DNA-based studies have described at least 44 mutations in the BCHE gene that cause primary hypocholinesterasemia, with the D70G ([Asp.
Copeland earned a BChE in Chemical Engineering from the University of Delaware and earned a Ph.
We a priori designated a "high-risk" allele for each polymorphism based on the expected functional impact with respect to acetylcholinesterase (AChE) inhibition (OP and carbamate insecticides; PON1, BCHE, FMO1, FM03, and GSTT1 polymorphisms) and ion channel stimulation [OC and pyrethroid insecticides; aldehyde dehydrogenase 3A1 (ALDH3A1) and GSTT1 polymorphisms].