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Literature summary extracted from

  • Andres, H.H.; Kolb, H.J.; Schreiber, R.J.; Weiss, L.
    Characterization of the active site, substrate specificity and kinetic properties of acetyl-CoA:arylamine N-acetyltransferase from pigeon liver (1983), Biochim. Biophys. Acta, 746, 193-201.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.5 3',5'-ADP kinetics Columba sp.
2.3.1.5 AMP kinetics Columba sp.
2.3.1.5 coenzyme A
-
Columba sp.
2.3.1.5 DTNB partly reversible by dithioerythritol Columba sp.
2.3.1.5 iodoacetamide
-
Columba sp.
2.3.1.5 iodoacetic acid
-
Columba sp.
2.3.1.5 p-chloromercuribenzoate
-
Columba sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.5 additional information
-
additional information kinetic data of various acetyl donors with 4-nitroaniline or aniline as acceptor amine and of various acceptor amines with acetyl-CoA as donor Columba sp.

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Anas sp.
-
duck
-
2.3.1.5 Columba sp.
-
pigeon
-
2.3.1.5 Meleagris gallopavo
-
-
-
2.3.1.5 Oncorhynchus mykiss
-
trout
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.5 acetyl-CoA + an arylamine = CoA + an N-acetylarylamine mechanism and characterization of active site Columba sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.5 liver
-
Meleagris gallopavo
-
2.3.1.5 liver
-
Oncorhynchus mykiss
-
2.3.1.5 liver
-
Anas sp.
-
2.3.1.5 liver
-
Columba sp.
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.5 additional information
-
-
Columba sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 additional information
-
Meleagris gallopavo ?
-
?
2.3.1.5 additional information
-
Oncorhynchus mykiss ?
-
?
2.3.1.5 additional information
-
Anas sp. ?
-
?
2.3.1.5 additional information the reaction proceeds via a covalent acetyl-enzyme intermediate Columba sp. ?
-
?
2.3.1.5 additional information no substrate: o-nitroaniline Columba sp. ?
-
?
2.3.1.5 additional information 4-nitroacetanilide, 4-nitrophenylacetate can replace acetyl-CoA Columba sp. ?
-
?
2.3.1.5 additional information no substrate: 2-amino-6-nitropyridine Columba sp. ?
-
?
2.3.1.5 p-nitroacetanilide + aniline
-
Columba sp. p-nitroaniline + acetanilide
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.5 additional information
-
pH-optimum depends on the nature of the acetyl acceptor amine Meleagris gallopavo
2.3.1.5 additional information
-
pH-optimum depends on the nature of the acetyl acceptor amine Oncorhynchus mykiss
2.3.1.5 additional information
-
pH-optimum depends on the nature of the acetyl acceptor amine Anas sp.
2.3.1.5 additional information
-
pH-optimum depends on the nature of the acetyl acceptor amine Columba sp.
2.3.1.5 5.9
-
4-nitroaniline Columba sp.
2.3.1.5 6.4
-
1,2-phenylenediamine Columba sp.
2.3.1.5 7
-
1,3-phenylenediamine Columba sp.
2.3.1.5 7.9
-
1,4-phenylenediamine Columba sp.
2.3.1.5 9.1
-
benzylamine Columba sp.