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Literature summary extracted from

  • Yamamura, E.; Sayama, M.; Kakikawa, M.; Mori, M.; Taketo, A.; Kodaira, K.
    Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli (2000), Biochim. Biophys. Acta, 1475, 10-16.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.118 expression as a hystidine tagged fusion protein Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.118 1-naphthol
-
Escherichia coli
2.3.1.118 2,6 dichloro-4-nitrophenol
-
Escherichia coli
2.3.1.118 2-naphthol
-
Escherichia coli
2.3.1.118 Acetylsalicylic acid
-
Escherichia coli
2.3.1.118 Harmaline
-
Escherichia coli
2.3.1.118 harmine
-
Escherichia coli
2.3.1.118 iodoacetamide
-
Escherichia coli
2.3.1.118 additional information inhibition by salicylic acid and N-ethylmaleimide is non competitive with acetyl-CoA and competitive with o-aminobenzoic acid Escherichia coli
2.3.1.118 N-ethylmaleimide
-
Escherichia coli
2.3.1.118 salicylic acid
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.118 0.36
-
p-Aminobenzoic acid
-
Escherichia coli
2.3.1.118 0.41
-
o-anisidine
-
Escherichia coli
2.3.1.118 0.48
-
o-aminobenzoic acid
-
Escherichia coli
2.3.1.118 0.54
-
p-Aminophenol
-
Escherichia coli
2.3.1.118 0.55
-
aniline
-
Escherichia coli
2.3.1.118 0.59
-
isoniazid
-
Escherichia coli
2.3.1.118 0.63
-
p-aminotoluene
-
Escherichia coli
2.3.1.118 0.83
-
p-anisidine
-
Escherichia coli
2.3.1.118 1.71
-
m-aminophenol
-
Escherichia coli
2.3.1.118 1.94
-
o-aminophenol
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.118 34000
-
2 * 34000, SDS-PAGE and DNA sequence Escherichia coli
2.3.1.118 60000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.118 acetyl-CoA + o-aminobenzoic acid Escherichia coli o-aminobenzoic acid is intermediate in the synthesis of tryptophane in E. coli CoA + N-acetyl-o-aminobenzoic acid
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.118 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.118 nickel affinity column chromatography, SDS-PAGE Escherichia coli

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.118 0.06
-
p-aminobenzoic acid Escherichia coli
2.3.1.118 0.09
-
aniline Escherichia coli
2.3.1.118 0.1
-
o-anisidine Escherichia coli
2.3.1.118 0.17
-
isoniazid Escherichia coli
2.3.1.118 0.25
-
p-aminotoluene Escherichia coli
2.3.1.118 0.28
-
m-aminophenol Escherichia coli
2.3.1.118 0.3
-
o-aminobenzoic acid Escherichia coli
2.3.1.118 0.33
-
p-aminophenol Escherichia coli
2.3.1.118 0.47
-
p-anisidine Escherichia coli
2.3.1.118 0.67
-
o-aminophenol Escherichia coli

Storage Stability

EC Number Storage Stability Organism
2.3.1.118 -20°C, 50 mM Tris-HCl, pH: 7.8, 10% glycerol, 1 month Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.118 acetyl-CoA + aniline N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetylaniline
-
?
2.3.1.118 acetyl-CoA + isoniazid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-isoniazid
-
?
2.3.1.118 acetyl-CoA + m-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-m-aminophenol
-
?
2.3.1.118 acetyl-CoA + o-aminobenzoic acid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-aminobenzoic acid
-
?
2.3.1.118 acetyl-CoA + o-aminobenzoic acid o-aminobenzoic acid is intermediate in the synthesis of tryptophane in E. coli Escherichia coli CoA + N-acetyl-o-aminobenzoic acid
-
?
2.3.1.118 acetyl-CoA + o-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-aminophenol
-
?
2.3.1.118 acetyl-CoA + o-anisidine N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-anisidine
-
?
2.3.1.118 acetyl-CoA + p-aminobenzoic acid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminobenzoic acid
-
?
2.3.1.118 acetyl-CoA + p-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminophenol
-
?
2.3.1.118 acetyl-CoA + p-aminotoluene N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminotoluene
-
?
2.3.1.118 acetyl-CoA + p-anisidine N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-anisidine
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.118 dimer 2 * 34000, SDS-PAGE and DNA sequence Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.118 37
-
maximum activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.118 7.4
-
maximum activity Escherichia coli