Literature summary extracted from

Correa-Basurto, J.; Bello, M.; Rosales-Hernandez, M.C.; Hernandez-Rodriguez, M.; Nicolas-Vazquez, I.; Rojo-Dominguez, A.; Trujillo-Ferrara, J.G.; Miranda, R.; Flores-Sandoval, C.A.
QSAR, docking, dynamic simulation and quantum mechanics studies to explore the recognition properties of cholinesterase binding sites (2014), Chem. Biol. Interact., 209, 1-13.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.1.1.8	(2Z)-4-[(2-aminophenyl)amino]-4-oxobut-2-enoic acid	one of the best inhibitors	Homo sapiens
3.1.1.8	(2Z)-4-[(4-nitrophenyl)amino]-4-oxobut-2-enoic acid	weak inhibition	Homo sapiens
3.1.1.8	1-(2-nitrophenyl)-1H-pyrrole-2,5-dione	weak inhibition	Homo sapiens
3.1.1.8	1-(2-nitrophenyl)pyrrolidine-2,5-dione	weak inhibition	Homo sapiens
3.1.1.8	1-(3-aminophenyl)pyrrolidine-2,5-dione	one of the best inhibitors	Homo sapiens
3.1.1.8	3-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)benzoic acid	one of the best inhibitors	Homo sapiens
3.1.1.8	4-[(2-aminophenyl)amino]-4-oxobutanoic acid	one of the best inhibitors	Homo sapiens
3.1.1.8	4-[(3-aminophenyl)amino]-4-oxobutanoic acid	weak inhibition	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.1.8	Homo sapiens	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.1.1.8	butyrylthiocholine + H2O	-	Homo sapiens	butyrate + thiocholine	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.1.1.8	BChE	-	Homo sapiens
3.1.1.8	butyrylcholinesterase	-	Homo sapiens

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Release 2023.1 (January 2023)