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Literature summary for 3.1.1.8 extracted from

  • Darvesh, S.; McDonald, R.S.; Darvesh, K.V.; Mataija, D.; Mothana, S.; Cook, H.; Carneiro, K.M.; Richard, N.; Walsh, R.; Martin, E.
    On the active site for hydrolysis of aryl amides and choline esters by human cholinesterases (2006), Bioorg. Med. Chem., 14, 4586-4599.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Butyrylcholine competitive to butyrylthiocholine Homo sapiens
butyrylthiocholine competitive to butyrylcholine Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information structure-activity relationships and kinetic studies, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyrylcholine + H2O
-
Homo sapiens choline + butyrate
-
?
butyrylthiocholine + H2O
-
Homo sapiens thiocholine + butyrate
-
?
additional information structure-activity relationships and kinetic studies, overview, the enzyme also shows an aryl acylamidase activity, EC 3.5.1.13, whereby it catalyzes the hydrolysis of amides of certain aromatic amines, BuChE shows high activity with larger N-(2-nitrophenyl)alkylamides, the ester and anilide substrates compete for the some catalytic site, no significant hydrolysis of the anilide takes place until the preferred choline ester hydrolysis is completed, overview Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
BuChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens
ChE
-
Homo sapiens
cholinesterase
-
Homo sapiens
More cf. EC 3.5.1.13 Homo sapiens