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Literature summary extracted from

  • Slemmon, J.R.; Salvaterra, P.M.; Roberts, E.
    Molecular characterization of choline acetyltransferase from Drosophila melanogaster (1984), Neurochem. Int., 6, 519-525.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.6 13000
-
 1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE Drosophila melanogaster
2.3.1.6 54000
-
 1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE Drosophila melanogaster
2.3.1.6 67000
-
 1 * 67000, SDS-PAGE Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.6 Drosophila melanogaster
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.6
-
 Drosophila melanogaster

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.3.1.6 dimer 1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE Drosophila melanogaster
2.3.1.6 monomer 1 * 67000, SDS-PAGE Drosophila melanogaster