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Literature summary extracted from

  • Malthe-Sorenssen, D.
    Molecular properties of choline acetyltransferase from different species investigated by isoelectric focusing and ion exchange adsorption (1976), J. Neurochem., 26, 861-865.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.6 0.66
-
 choline
-
 Platyrrhini
2.3.1.6 0.88
-
 choline
-
 Mus musculus
2.3.1.6 0.92
-
 choline
-
 Oryctolagus cuniculus
2.3.1.6 3.5
-
 choline
-
 Torpedo sp.

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.6 Mus musculus
-
 3 enzyme forms
-
2.3.1.6 Oryctolagus cuniculus
-
-
-
2.3.1.6 Platyrrhini
-
 3 enzyme forms
-
2.3.1.6 Torpedo sp.
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.6 brain
-
 Mus musculus
-
2.3.1.6 brain
-
 Oryctolagus cuniculus
-
2.3.1.6 brain
-
 Platyrrhini
-
2.3.1.6 electric organ
-
 Torpedo sp.
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.6 acetyl-CoA + choline
-
 Mus musculus acetylcholine + CoA
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Oryctolagus cuniculus acetylcholine + CoA
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Platyrrhini acetylcholine + CoA
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Torpedo sp. acetylcholine + CoA
-
 ?