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Literature summary extracted from

  • Golicnik, M.; Sinko, G.; Simeon-Rudolf, V.; Grubic, Z.; Stojan, J.
    Kinetic Model of ethopropazine Interaction with horse serum butyrylcholinesterase and its docking into the active site (2002), Arch. Biochem. Biophys., 398, 23-31.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.8 ethopropazine inhibits at low substrate concentrations, inhibition mechanism Equus caballus

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 Equus caballus
-
choline + butyrate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.8 Equus caballus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.8
-
Equus caballus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.8 serum
-
Equus caballus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.8 acetylthiocholine iodide + H2O
-
Equus caballus thiocholine iodide + acetate
-
?
3.1.1.8 butyrylcholine + H2O
-
Equus caballus choline + butyrate
-
?
3.1.1.8 butyrylthiocholine iodide + H2O
-
Equus caballus thiocholine iodide + butyrate
-
?

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.8 25 37 activity at 25°C at low substrate concentrations is higher than at 37°C Equus caballus