3.1.1.8: cholinesterase
This is an abbreviated version!
For detailed information about cholinesterase, go to the full flat file.
Word Map on EC 3.1.1.8
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3.1.1.8
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ache
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alzheimer
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cholinergic
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acetylcholine
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organophosphate
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nerve
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dementia
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pesticide
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poison
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donepezil
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organophosphorus
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insecticide
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erythrocyte
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physostigmine
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deficit
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atropine
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neuromuscular
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carbamate
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rivastigmine
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muscarinic
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intoxication
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neurotoxicity
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amyloid
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nicotinic
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galantamine
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tacrine
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neuroprotective
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oxime
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placebo
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innervation
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carboxylesterase
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chlorpyrifos
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soman
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memantine
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caregiver
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mini-mental
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antipsychotic
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esterases
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parathion
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placebo-controlled
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myasthenia
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anticholinergic
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paraoxon
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dfp
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scopolamine
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antidote
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gravis
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subscale
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delirium
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medicine
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pharmacology
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environmental protection
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drug development
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diagnostics
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analysis
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hallucinations
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biotechnology
- 3.1.1.8
-
ache
- alzheimer
-
cholinergic
- acetylcholine
-
organophosphate
- nerve
- dementia
-
pesticide
-
poison
- donepezil
-
organophosphorus
-
insecticide
- erythrocyte
- physostigmine
- deficit
- atropine
- neuromuscular
- carbamate
- rivastigmine
-
muscarinic
-
intoxication
-
neurotoxicity
-
amyloid
-
nicotinic
- galantamine
- tacrine
-
neuroprotective
- oxime
-
placebo
-
innervation
- carboxylesterase
- chlorpyrifos
- soman
- memantine
-
caregiver
-
mini-mental
-
antipsychotic
- esterases
- parathion
-
placebo-controlled
- myasthenia
-
anticholinergic
- paraoxon
- dfp
- scopolamine
-
antidote
- gravis
-
subscale
- delirium
- medicine
- pharmacology
- environmental protection
- drug development
- diagnostics
- analysis
- hallucinations
- biotechnology
Reaction
Synonyms
acyl choline acylhydrolase, acylcholine acyl-hydrolase, Acylcholine acylhydrolase, atypical cholinesterase, BChE, benzoylcholinesterase, BoBChE, BTCh, BTChI-ChE, BtChoEase, BuChE, butyrocholinesterase, butyryl-ChE, butyrylChE, butyrylcholine esterase, butyrylcholine-hydrolyzing enzyme, butyrylcholinesterase, butyrylcholinesterase K, calcium-activated butyrylcholinesterase, ChE, ChE-II, CholE, choline esterase, choline esterase II (unspecific), cholinesterase, dBChE, DjChE, Djche1, Djche2, EQ-BCHE, eqBChE, EqBuChE, esterase, butyrylcholine, esterase, choline, hBChE, HuBChE, mBuChE I, mBuChE II, monomeric butyrylcholinesterase I, monomeric butyrylcholinesterase II, More, non specific cholinesterase, non-specific cholinesterase, PChE, planarian cholinesterase, plasma cholinesterase, plasma esterase, plasmatic cholinesterase, PoBChE, propionylcholinesterase, pseudo choline esterase, pseudo cholinesterase, pseudocholinesterase, PTChI-ChE, rBChE, serum cholinesterase
ECTree
3.1.1.8 cholinesteraseAdvanced search results
results (
results (Engineering
Engineering on EC 3.1.1.8 - cholinesterase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F398I
site-directed mutagenesis, altered structure compared to wild-type enzyme
G117H/P285L/F398I
site-directed mutagenesis, altered structure compared to wild-type enzyme
G117S
site-directed mutagenesis, altered structure compared to wild-type enzyme
G117S/F398I
site-directed mutagenesis, altered structure compared to wild-type enzyme
G117S/P285L
site-directed mutagenesis, altered structure compared to wild-type enzyme
G117S/P285L/F398I
site-directed mutagenesis, altered structure compared to wild-type enzyme
P285L
site-directed mutagenesis, altered structure compared to wild-type enzyme
P285L/F398I
site-directed mutagenesis, altered structure compared to wild-type enzyme
A199S/F227A/S287G/A328W/E441D
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the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A199S/F227A/S287G/A328W/Y332G/E441D
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the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A199S/S287G/A328W/Y332G
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the mutant has significantly lower kcat and KM values against acetylcholine than the wild type enzyme
A328F
A328G
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328I
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328W
A328W/Y332A
A328Y
A539T
D70G
E197Q
F329A
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
G117H
G333C
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naturally occuring mutation, the mutant shows about 80% decreases enzyme activity compared to the wild-type enzyme
L286W
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
V288W
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
W430A
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retained substrate activation, strongly reduced affinity for tetramethylammonium, bimolecular rate constant for reaction with diisopropyl fluorophosphate is reduced 10000fold
W82A
Y332A
additional information
A328F
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328F
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
A328W
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328W
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
A328W/Y332A
mutant reduces cocain burden in tissues, accelerates plasma clearance by 20fold and prevents cocaine-induced hyperactivity in mice
A328W/Y332A
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the engineered recombinant cocaine hydrolase displays increased cocaine hydrolysis ability and increased affinity to the organophosphate pesticides paraoxon and malaoxon compared to the wild-type enzyme, overview
A328Y
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
A328Y
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
A539T
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
D70G
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site-directed mutagenesis, peripheral site mutant, altered kinetics compared to the wild-type enzyme and no substrate activation, overview
D70G
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
E197Q
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
G117H
the mutation leads to the creation of organophosphylate hydrolase activity
W82A
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apparent substrate activation at butytylthiocholine concentrations greater than 2 mM
Y332A
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mutant enzyme retains activity at pH 5 under conditions of excess substrate similar to the wild-type enzyme
Y332A
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the mutant is more sensitive to aryl phenothiazine carbamate inhibitors and deactivation, i.e. 4-biphenyl phenothiazine carbamate, compared to the wild-type enzyme
additional information
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construction of a a quadruple mutant cocaine hydrolase CocH with improved catalytic efficiency for cocaine, the mutant enzyme is expressed as albumin fusion protein and introduced in rats, male and female Wistar rats, showing enzyme activity but also high enzyme decay rates
additional information
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genotyping in Southern Brasilian population and polymorpshisms of the BCHE alleles, overview
additional information
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mutation of a conserved arginine in neuroligin and BChE induces misfolding and retention in the endoplasmic reticulum
additional information
generation of a truncated L530stop, 4 sugars off HuBChE mutant. The deleted glycosylation sites N17/455/481/486 unmask N485 for glycosylation, so that the rHuBChE contains 6 glycans. N485 is not glycated in plasma-derived HuBChE
additional information
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generation of a truncated L530stop, 4 sugars off HuBChE mutant. The deleted glycosylation sites N17/455/481/486 unmask N485 for glycosylation, so that the rHuBChE contains 6 glycans. N485 is not glycated in plasma-derived HuBChE
additional information
preparation of copolymer-rhBChE complexes (C-BCs) based on one of nine different copolymers, from combinations of three molecular weights (MW) of poly-L-lysine (PLL, high MW, 30-70 kDa, medium MW, 15-30 kDa, low MW, 4-15 kDa) and three grafting ratios of poly(ethylene glycol) (PEG, 2:1, 10:1, 20:1) for complexing of the enzyme as improved bioscavenger for organophosphorus toxicants, method evaluation, overview. Similar sensitivity to in vitro inhibition of BChE activity is noted with the free enzyme and various C-BCs
additional information
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preparation of copolymer-rhBChE complexes (C-BCs) based on one of nine different copolymers, from combinations of three molecular weights (MW) of poly-L-lysine (PLL, high MW, 30-70 kDa, medium MW, 15-30 kDa, low MW, 4-15 kDa) and three grafting ratios of poly(ethylene glycol) (PEG, 2:1, 10:1, 20:1) for complexing of the enzyme as improved bioscavenger for organophosphorus toxicants, method evaluation, overview. Similar sensitivity to in vitro inhibition of BChE activity is noted with the free enzyme and various C-BCs
additional information
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recombinant regulated BChE (rrBChE) differs from the wild-type in that it contains plant-type complex N-glycans, including an alpha-1,3 linked core fucose, and a beta-1,2 xylose, and lacking a terminal sialic acid. Despite this difference, rrBChE is demonstrated to be an effective stoichiometric bioscavenger for five different organophosphorous nerve agents in vitro
