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Literature summary for 3.1.1.7 extracted from

  • Golicnik, M.; Stojan, J.
    Multi-step analysis as a tool for kinetic parameter estimation and mechanism discrimination in the reaction between tight-binding fasciculin 2 and electric eel acetylcholinesterase (2002), Biochim. Biophys. Acta, 1597, 164-172.
    View publication on PubMed
Search for more literature for 3.1.1.7

Inhibitors

Inhibitors Comment Organism Structure
fasciculin-2 potent inhibitor Electrophorus electricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylcholine + H2O Electrophorus electricus
-
 choline + acetate
-
 ?

Organism

Organism UniProt Comment Textmining
Electrophorus electricus
-
 electric eel
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
-
 Electrophorus electricus choline + acetate
-
 ?
additional information complex with fasciculin-2 exhibits hydrolytic activity in a buryrylcholinesterase-like kinetics, the switch appears to be a consequence of steric obstruction, but also the consequence of subtle rapid conformational changes around the catalytic site Electrophorus electricus ?
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.33 0.36 fasciculin-2 23°C, pH 8 Electrophorus electricus