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evolution
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as one of the most ancient true cholinesterases, DjChE provides insight into the evolution of a hybrid enzyme before the separation into distinct AChE and BChE enzymes found in higher vertebrates
malfunction
compound C547 and pyridostigmine show efficiency to reduce muscle weakness symptoms and ability to activate contractions of urinary bladder in a rat model of autoimmune myasthenia gravis (MG). At a dose effectively reducing MG symptoms, C547 does not affect activity of rat urinary bladder, while at equipotent dose, pyridostigmine causes a significant increase in tonus and force of spontaneous contractions of bladder wall
malfunction
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DjChE inhibition affects planarian behavior, inhibitors delay the reaction of planarians to heat stress. Simultaneous knockdown of both Djche genes by RNAi similarly results in a delayed heat stress response. Chemical inhibition of DjChE activity increases the worms' ability to adhere to a substrate. But increased substrate adhesion is not observed in Djche1/Djche2 (RNAi) animals or in inhibitor-treated day 11 regenerates, suggesting this phenotype may be modulated by other mechanisms besides ChE inhibition
physiological function
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low paraoxonase-1 catalytic efficiency and low plasma PON1 activity in human are associated with BuChE inhibition among organophosphate-exposed agricultural pesticide handlers
physiological function
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a key enzyme of the cholinergic nervous system
physiological function
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a key enzyme of the cholinergic nervous system
physiological function
background activity of BChE in the bladder might be sufficient to compensate for partial inhibition of AChE (EC 3.1.1.7), in contrast to skeletal muscle. Functional role of BChE might be different in the urinary bladder of rat and human
physiological function
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BChE is implicated in lipid metabolism and various human diseases such as liver damage, diabetes, Alzheimer's disease (AD) and liver metastasis. BChE is also responsible for detoxifying xenobiotics such as organophosphates and cocaine, and its engineered mutants have drawn a great deal of interest as detoxifying therapeutics. Thus, the quantification of BChE activity and its inhibition are highly important in drug discovery and clinical diagnostics
physiological function
butyrylcholinesterase (BChE) is mainly present in plasma and generally hydrolyzes butyrylthiocholine at a higher rate than acetylthiocholine but unlike acetylcholinesterase (AChE, EC 3.1.1.7), it is not inhibited by high concentrations of substrate. In cattle, 90% of cholinesterase enzyme activity is represented by AChE in erythrocytes with very low plasma BChE values
physiological function
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butyrylcholinesterase is a serine hydrolase loosely related to the mammalian cholinergic system. It shows a nearly ubiquitous distribution among tissues and is abundant in plasma. In plasma, BChE protects the neurotransmitter function of its sister enzyme acetylcholinesterase (AChE, EC 3.1.1.7) by neutralizing toxins (including neuroactive pesticides, drugs, and a few other chemicals like food additives) before they reach AChE, while in the central nervous system as well as at the neuromuscular junction it serves as a backup to AChE by breaking down acetylcholine that has diffused out of the synaptic cleft
physiological function
human butyrylcholinesterase (HuBChE) is an efficient bioscavenger of organophosphorus nerve agents
physiological function
PoBChE hydrolyzes acetylthiocholine slightly faster than butyrylthiocholine, but is sensitive to BChE-specific inhibitors
physiological function
the enzyme is thought to be primarily responsible for detoxification reactions in the serum, liver, lungs, and intestinal mucosa
physiological function
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the majority of Dugesia japonica cholinesterase (DjChE) activity departs from conventional AChE and BChE classifications
additional information
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cholinesterase does not ungergo disease-related modification in the primary structure during Alzheimer's disease
additional information
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analysis of the catalytic mechanism, especially the difference in the active sites of BChE (PDB ID 1P0M) and AChE (PDB ID 1B41). Usage of BChE-FP, molecular probe specific to butyrylcholinesterase, shows good properties: it exhibits good specificity and can discriminate BChE from AChE, shows about 275fold fluorescence intensity enhancement in pure aqueous solution, and shows about 100fold greater binding affinity towards BChE than and comparable catalytic efficiency to the widely used substrate acetylthiocholine iodide
additional information
catalysis takes place in a 20-A deep active site gorge and involves a catalytic triad of serine, histidine, and glutamate residues located near the bottom of the gorge, denoted the acylation or A-site. The region near the rim of the gorge has been denoted the peripheral site or P-site
additional information
construction of Hupresin affinity resin by coupling the huprine (inhibitor) ligand to Sepharose 4B via a 10-atom spacer between the Sepharose beads and the ligand. The spacer extends the ligand out of the Sepharose backbone, making room for the BChE protein to interact with the ligand. Hupresin compared to procainamide affinity gel for purifying BChE, method evaluation, overview. Hupresin is superior to procainamide-resin for purification of BChE, but is not suitable for purifying native acetylcholinesterase, AChE (EC 3.1.1.7), because Hupresin binds AChE so tightly that AChE is not released with buffers, but is desorbed with denaturing solvents such as 50% acetonitrile or 1% trifluoroacetic acid. Procainamide-Sepharose will continue to be useful for purification of AChE
additional information
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construction of Hupresin affinity resin by coupling the huprine (inhibitor) ligand to Sepharose 4B via a 10-atom spacer between the Sepharose beads and the ligand. The spacer extends the ligand out of the Sepharose backbone, making room for the BChE protein to interact with the ligand. Hupresin compared to procainamide affinity gel for purifying BChE, method evaluation, overview. Hupresin is superior to procainamide-resin for purification of BChE, but is not suitable for purifying native acetylcholinesterase, AChE (EC 3.1.1.7), because Hupresin binds AChE so tightly that AChE is not released with buffers, but is desorbed with denaturing solvents such as 50% acetonitrile or 1% trifluoroacetic acid. Procainamide-Sepharose will continue to be useful for purification of AChE
additional information
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Djche1 and Djche2 enzyme structure homology modelling using Torpedo californica AChE as the template (PDB IDs 2cek and 2w6c, respectively)
additional information
enzyme homology modeling, molecular modeling, overview
additional information
enzyme structure homology modelling, molecular dynamics simulations on the structures of enzyme-substrate complexes using the crystal structures of AChE (PDB ID 1B41), and BChE (PDB IDs 2XQF and 1P0P), molecular docking, overview. The positively charged amino-group of the substrates (heroin and 6-monoacetylmorphine) is placed in the choline-binding site near Trp82 in BChE and CocH1 or Trp86 in AChE. The binding models of heroin and 6-monoacetylmorphine in the corresponding enzyme-substrate complexes are optimized by performing the energy minimization
additional information
enzyme-ligand docking study, overview
additional information
molecular dynamics modeling, homology structure modelling using diethylphosphorylated wild-type human BChE structure, PDB ID 1XLW, structure comparisons, overview. BChE protein has the catalytic triad residues Ser198, Glu325, His438, the choline binding site Trp82, the peripheral site residues Asp70, Tyr332, and the acyl binding pocket Leu286, Val288, Trp231. The oxyanion hole residue is Ser117 in BoBChE
additional information
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molecular dynamics modeling, homology structure modelling using diethylphosphorylated wild-type human BChE structure, PDB ID 1XLW, structure comparisons, overview. BChE protein has the catalytic triad residues Ser198, Glu325, His438, the choline binding site Trp82, the peripheral site residues Asp70, Tyr332, and the acyl binding pocket Leu286, Val288, Trp231. The oxyanion hole residue is Ser117 in BoBChE
additional information
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structure and activity comparisons of Oryzsa sativa and Homo sapiens enzymes, overview
additional information
the concentration of active sites in PoBChE is determined by titration with 7-(O,O-diethyl-phosphinyloxy)-1-methylquinolinium methylsulfate (DEPQ)
additional information
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the concentration of active sites in PoBChE is determined by titration with 7-(O,O-diethyl-phosphinyloxy)-1-methylquinolinium methylsulfate (DEPQ)