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Literature summary for 3.1.1.8 extracted from

  • Liang, D.; Blouet, J.P.; Borrega, F.; Bon, S.; Massoulie, J.
    Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase (2009), FEBS J., 276, 94-108.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
7-[(diethoxyphosphoryl)oxy]-1-methylquinolinium iodide an irreversible inhibitor Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylthiocholine + H2O Homo sapiens
-
acetate + thiocholine
-
?
butyrylthiocholine + H2O Homo sapiens
-
butyrate + thiocholine
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-
muscle
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylthiocholine + H2O
-
Homo sapiens acetate + thiocholine
-
?
butyrylthiocholine + H2O
-
Homo sapiens butyrate + thiocholine
-
?

Subunits

Subunits Comment Organism
More butyrylcholinesterase consists of a catalytic domain of approximately 500 residues, followed by C-terminal tail t peptide, the t peptide plays an important role in the biosynthesis of cholinesterases, particularly their folding and export Homo sapiens
More the enzyme possesses a characteristic C-terminal tail t peptide, which is not required for BChE cholinesterase activity, overview Homo sapiens
oligomer BChE forms monomers, dimers and tetramers Homo sapiens

Synonyms

Synonyms Comment Organism
BChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens