Literature summary for 3.1.1.7 extracted from

Nemukhin, A.V.; Lushchekina, S.V.; Bochenkova, A.V.; Golubeva, A.A.; Varfolomeev, S.D.
Characterization of a complete cycle of acetylcholinesterase catalysis by ab initio QM/MM modeling (2008), J. Mol. Model., 14, 409-416.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis, overview	Tetronarce californica

Protein Variants

Protein Variants	Comment	Organism
E202Q	structure analysis	Tetronarce californica

Organism

Organism	UniProt	Comment	Textmining
Tetronarce californica	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
acetylcholine + H2O = choline + acetate	reaction mechanism, active site structure, the catalytic triad comprises the residues Ser203, His447, Glu334, residues Ser203 and His447 are directly involved in the reaction, serving as nucleophilic attacking group and general acid base catalytic elements, respectively, at the acylation stage of the enzymatic reaction. Modern molecular modeling using tools including molecular docking, molecular dynamics (MD), quantum chemistry and the combined quantum mechanical-molecular mechanical method, overview	Tetronarce californica	a

Synonyms

Synonyms	Comment	Organism
acetylcholinesterase	-	Tetronarce californica
AChE	-	Tetronarce californica

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Release 2023.1 (January 2023)