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Literature summary extracted from

  • Carbini, L.A.; Hersh, L.B.
    Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis (1993), J. Neurochem., 61, 247-253.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.6 H268L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster
2.3.1.6 H268N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster
2.3.1.6 H393L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster
2.3.1.6 H393N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster
2.3.1.6 H426L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster
2.3.1.6 H426N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.6 0.014
-
 CoA enzyme mutant H268N Drosophila melanogaster
2.3.1.6 0.016
-
 CoA
-
 Drosophila melanogaster
2.3.1.6 0.017
-
 CoA enzyme mutant H393N Drosophila melanogaster
2.3.1.6 0.04
-
 CoA enzyme mutant H268L Drosophila melanogaster
2.3.1.6 0.67
-
 Acetylcholine enzyme mutant H393N Drosophila melanogaster
2.3.1.6 1.7
-
 Acetylcholine enzyme mutant H268L Drosophila melanogaster
2.3.1.6 2.1
-
 Acetylcholine
-
 Drosophila melanogaster
2.3.1.6 2.7
-
 Acetylcholine enzyme mutant H268N Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.6 68000
-
 1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE Drosophila melanogaster
2.3.1.6 68000
-
 1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.6 Caenorhabditis elegans
-
 nematode
-
2.3.1.6 Drosophila melanogaster
-
-
-
2.3.1.6 Rattus norvegicus
-
-
-
2.3.1.6 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.6 retina
-
 Rattus norvegicus
-

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
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Rattus norvegicus acetylcholine + CoA
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Sus scrofa acetylcholine + CoA
-
 ?
2.3.1.6 acetyl-CoA + choline
-
 Caenorhabditis elegans acetylcholine + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.6 monomer 1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE Drosophila melanogaster
2.3.1.6 monomer 1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE Rattus norvegicus