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Literature summary for 2.3.1.6 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
Search for more literature for 2.3.1.6

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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]

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

Molecular Weight [Da]

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

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
retina
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + choline
-
 Drosophila melanogaster acetylcholine + CoA
-
 ?
acetyl-CoA + choline
-
 Rattus norvegicus acetylcholine + CoA
-
 ?
acetyl-CoA + choline
-
 Sus scrofa acetylcholine + CoA
-
 ?
acetyl-CoA + choline
-
 Caenorhabditis elegans acetylcholine + CoA
-
 ?

Subunits

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