Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. (updated: Oct. 10, 2018)
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No sequence conservation computed yet.
Total structural coverage: 91%
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The reference OMIM entry for this protein is 177400
Butyrylcholinesterase; bche
Pseudocholinesterase e1; che1
Acylcholine acylhydrolase butyrylcholinesterase deficiency, included
Acholinesterasemia, included
Suxamethonium sensitivity, included
Pseudocholinesterase deficiency, included
Apne
CLONING
Lockridge et al. (1987) concluded that the 4 subunits of cholinesterase are identical and that each contains 574 amino acids and 9 carbohydrate chains attached to 9 asparagines. Prody et al. (1987) isolated and characterized full-length cDNA clones for pseudocholinesterase (butyrylcholinesterase) from human fetal tissues. McTiernan et al. (1987) screened a cDNA library from human basal ganglia with oligonucleotide probes corresponding to the amino acid sequence of human serum cholinesterase (EC 3.1.1.8), which is also known as acylcholine acylhydrolase. There were 1,722 basepairs of the coding sequence corresponding to the protein found circulating in human serum. The amino acid sequence deduced from the cDNA exactly matched the 574-amino acid sequence of human serum cholinesterase; therefore, the clones represented cholinesterase rather than acetylcholinesterase (ACHE;
100740). Hybridization of genomic DNA blots suggested that a single gene, or very few genes, code for cholinesterase. The amino acid sequences of cholinesterase in brain and serum are apparently identical. Cholinesterase is present in particularly high levels in embryonic and fetal human brain as well as in nervous system tumors such as glioblastomas, neuroblastomas, and meningiomas. The widespread expression in early differentiation suggests development-related functions for this protein.
MAPPING
On the basis of dosage effects, Arias et al. (1985) suggested that CHE1 is located at 3q25.2 and that ceruloplasmin (CP;
117700) and TF are nearer the centromere. Using a cDNA clone as a probe for in situ hybridization, Soreq et al. (1987) mapped the CHE1 gene to 3q21-q26. Lapidot-Lifson et al. (1989) studied the coamplification of butyrylcholinesterase and acetylcholinesterase (
100740) in disorders of platelet production and in leukemia patients. This may indicate that the 2 genes are linked. Gnatt et al. (1990) found that cDNAs made from BCHE mRNA in glioblastoma and nerve blastoma cells map to the same site on 3q where the serum protein polymorphism maps. Furthermore, the asp70-to-gly mutation, which is responsible for the 'atypical' butyrylcholinesterase that is deficient in its capacity to hydrolyze succinylcholine, was identified in an mRNA isolated from glioblastoma tissue. Both Allderdice et al. (1991) and Gaughan et al. (1991) confirmed localization of the BCHE gene on 3q26. For the study of localization by in situ hybridization in a chromosomal rearrangement, Allderdice et al. (1991) used a different cDNA probe from that used by Soreq et al. (1987). Gaughan et al. (1991) used a PCR-derived probe that included the active site region to give a single hybridization signal by in situ hybridization and refined the localization to 3q26.1-q26.2.
CLINICAL FEATURES
Mutant alleles at the CHE1 locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage. The dibucaine number (percentage inhibition by dibucaine) identifies 3 genotypes (Kalow and Genest, 1957). Two further alleles are a silent gene and an allele identified by fluoride inhibition. Heterogeneity of the 'silent' cholinesterase genes was indicated by the studies of Rubinstein et ...
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Subscribe to this protein entry history
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 177400 was added.
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).