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Literature summary for 3.1.1.8 extracted from

  • Yang, S.H.; Sun, Q.; Xiong, H.; Liu, S.Y.; Moosavi, B.; Yang, W.C.; Yang, G.F.
    Discovery of a butyrylcholinesterase-specific probe via a structure-based design strategy (2017), Chem. Commun. (Camb.), 53, 3952-3955 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information donepezil is a specific AChE inhibitor Homo sapiens
tacrine tacrine has similar inhibition potencies against BChE and AChE Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Homo sapiens
0.00301
-
BChE-FP pH 7.0, 30°C Homo sapiens
0.3081
-
acetylthiocholine pH 7.0, 30°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
butyrylcholine + H2O Homo sapiens
-
choline + butyrate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
PANC-1 cell endogenous BChE is located in the cytoplasm of PANC-1 cells Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylthiocholine + H2O 100fold lower binding activity compared to butyrylthiocholine Homo sapiens thiocholine + acetate
-
?
BChE-FP + H2O structure-based design and application of a fluorogenic molecular probe, BChE-FP, specific to butyrylcholinesterase (BChE). This compound is rationally designed by mimicking the native substrate and optimized stepwise by manipulating the steric feature and the reactivity of the designed probe targeting the structural difference of the active pockets of BChE and acetylcholinesterase (AChE). The refined probe, BChE-FP, exhibits high specificity toward BChE compared to AChE, producing about 275fold greater fluorescence enhancement upon the catalysis by BChE, molecular docking simulation, overview. The proximity of Ser198 to the carbonyl group of BChE-FP is about 4.3 A in the BChE active site, whereas the proximity of Ser203 to the carbonyl group of BChE-FP is about 7.4 A in the AChE active site. The binding affinity of BChE-FP with BChE is B100fold greater than that of acetylthiocholine, while the catalytic constant for BChE-FP is 190fold lower than that of acetylthiocholine Homo sapiens ?
-
?
butyrylcholine + H2O
-
Homo sapiens choline + butyrate
-
?
butyrylthiocholine + H2O
-
Homo sapiens thiocholine + butyrate
-
?

Synonyms

Synonyms Comment Organism
BChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.75
-
BChE-FP pH 7.0, 30°C Homo sapiens
334.9
-
acetylthiocholine pH 7.0, 30°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00001069
-
tacrine pH 7.0, 30°C Homo sapiens

General Information

General Information Comment Organism
additional information 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 Homo sapiens
physiological function 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 Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1087
-
BChE-FP pH 7.0, 30°C Homo sapiens
1668.4
-
acetylthiocholine pH 7.0, 30°C Homo sapiens