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Literature summary for extracted from

  • Pathak, R.; Kanwar, S.S.; Sanyal, S.N.
    Kinetic behaviour of the multiple molecular forms of acetylcholinesterase in the human term placenta (2006), Int. J. Mendel, 23, 57-58.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
additional information kinetics of multiple molecular forms of the enzyme Homo sapiens


Organism UniProt Comment Textmining
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
placenta multiple molecular forms of the enzyme in different tissue fractions, i.e. the 2000 x g supernatant, the low salt-solubilizable fraction, and the detergent-solubilizable fraction, overview Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
term placenta low salt-solubilizable fraction Homo sapiens
term placenta detergent-solubilizable fraction Homo sapiens
term placenta 2000 x g supernatant fraction Homo sapiens

Substrates and Products (Substrate)

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


Synonyms Comment Organism
Homo sapiens