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Literature summary extracted from

  • Chinnadurai, R.K.; Saravanaraman, P.; Boopathy, R.
    Understanding the molecular mechanism of aryl acylamidase activity of acetylcholinesterase - An in silico study (2015), Arch. Biochem. Biophys., 580, 1-13 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.13 BW284c51 dual site binder, interacts with PAS and the active site of acetylcholinesterase, thus inhibiting both the activities (esterase and aryl acylamidase) Homo sapiens
3.5.1.13 additional information by molecular docking studies the most favourable binding site of aryl acylamidase substrates and serotonin is identified as the side door of acetylcholinesterase. Propidium, a peripheral anionic site binder blocks the main door without affecting the side door, which explains its ineffectiveness in inhibiting aryl acylamidase Homo sapiens
3.5.1.13 serotonin serotonin inhibits aryl acylamidase while remaining ineffective against the esterase activity. It interacts with D74, N87, L76 and T83 residues of the side door Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.13 Homo sapiens P22303 cf. EC 3.1.1.7
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.13 2-nitroacetanilide + H2O acetylcholinesterase exhibits two different activities: esterase and aryl acylamidase Homo sapiens 2-nitroaniline + acetate
-
 ?
3.5.1.13 2-nitrotrifluoroacetanilide + H2O acetylcholinesterase exhibits two different activities: esterase and aryl acylamidase Homo sapiens 2-nitroaniline + trifluoroacetic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.13 AAA
-
 Homo sapiens