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Literature summary extracted from

  • Habert, E.; Birman, S.; Mallet, J.
    High-level synthesis and fate of acetylcholine in baculovirus-infected cells: characterization and purification of recombinant rat choline acetyltransferase (1992), J. Neurochem., 58, 1447-1453.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.6 expression in Spodoptera frugiperda Sf9 cells Rattus norvegicus
2.3.1.6 expression in Spodoptera frugiperda Sf9 cells using a baculovirus expression system Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.6 0.221
-
 acetyl-CoA
-
 Rattus norvegicus
2.3.1.6 0.299
-
 choline
-
 Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.6 68500
-
 1 * 68500, SDS-PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.6 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.6 phosphoprotein rat choline acetyltransferase is phosphorylated in Sf9 cells Rattus norvegicus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.6
-
 Rattus norvegicus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.6 0.19
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.6 acetyl-CoA + choline
-
 Rattus norvegicus acetylcholine + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.6 monomer 1 * 68500, SDS-PAGE Rattus norvegicus