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Literature summary for 3.1.1.7 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

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
20.4
-
term placenta low salt-solubilizable fraction Homo sapiens
22.4
-
term placenta detergent-solubilizable fraction Homo sapiens
3.94
-
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

Synonyms Comment Organism
AChE
-
Homo sapiens