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

Search for more literature for 3.1.1.7

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
3.94	-	term placenta 2000 x g supernatant fraction	Homo sapiens
20.4	-	term placenta low salt-solubilizable fraction	Homo sapiens
22.4	-	term placenta detergent-solubilizable 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

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Release 2023.1 (January 2023)