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Literature summary for 3.1.1.8 extracted from

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

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-(acetamido)N,N,N-trimethylanilinium + H2O
-
Homo sapiens ?
-
?
benzoylthiocholine + H2O
-
Homo sapiens ?
-
?
butyrylcholine + H2O
-
Homo sapiens butyrate + choline
-
?
butyrylthiocholine + H2O
-
Homo sapiens butyrate + thiocholine
-
?

Synonyms

Synonyms Comment Organism
BuChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens
ChE
-
Homo sapiens