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Literature summary for 2.3.1.118 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
Search for more literature for 2.3.1.118

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + aniline N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetylaniline
-
 ?
acetyl-CoA + isoniazid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-isoniazid
-
 ?
acetyl-CoA + m-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-m-aminophenol
-
 ?
acetyl-CoA + o-aminobenzoic acid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-aminobenzoic acid
-
 ?
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
-
 ?
acetyl-CoA + o-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-aminophenol
-
 ?
acetyl-CoA + o-anisidine N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-o-anisidine
-
 ?
acetyl-CoA + p-aminobenzoic acid N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminobenzoic acid
-
 ?
acetyl-CoA + p-aminophenol N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminophenol
-
 ?
acetyl-CoA + p-aminotoluene N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-aminotoluene
-
 ?
acetyl-CoA + p-anisidine N-acetyltransferase activity, ping-pong bi bi mechanism Escherichia coli CoA + N-acetyl-p-anisidine
-
 ?

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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