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Literature summary extracted from

  • Masson, P.
    Time-dependent kinetic complexities in cholinesterase-catalyzed reactions (2012), Biochemistry, 77, 1147-1161.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.8 expressed in CHO-K1 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.8 A328C the mutation leads to hysteresis with butyrylthiocholine Homo sapiens
3.1.1.8 G117H/A199E the mutation leads to hysteresis with benzoylthiocholine Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.8 phenyl trimethyl ammonium specific inhibitor Homo sapiens
3.1.1.8 procainamide specific inhibitor Homo sapiens

Natural Substrates/ Products (Substrates)

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

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 3-(acetamido)N,N,N-trimethylanilinium + H2O
-
 Homo sapiens ?
-
 ?
3.1.1.8 benzoylthiocholine + H2O
-
 Homo sapiens ?
-
 ?
3.1.1.8 butyrylcholine + H2O
-
 Homo sapiens butyrate + choline
-
 ?
3.1.1.8 butyrylthiocholine + H2O
-
 Homo sapiens butyrate + thiocholine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.8 BuChE
-
 Homo sapiens
3.1.1.8 butyrylcholinesterase
-
 Homo sapiens
3.1.1.8 ChE
-
 Homo sapiens