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Literature summary extracted from

  • Kubiak, X.; Li de la Sierra-Gallay, I.; Chaffotte, A.F.; Pluvinage, B.; Weber, P.; Haouz, A.; Dupret, J.M.; Rodrigues-Lima, F.
    Structural and biochemical characterization of an active arylamine N-acetyltransferase possessing a non-canonical Cys-His-Glu catalytic triad (2013), J. Biol. Chem., 288, 22493-22505.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.5 expressed in Escherichia coli BL21 cells Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.5 hanging drop vapor diffusion method, using 1.6 M sodium citrate, pH 6.5, 0.28 M NDSB-221 as additive Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.5 E123D the catalytic efficiency is 1.6-4.4 times higher than that of the wild type enzyme Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.5 iodoacetamide
-
Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.5 0.05
-
acetyl-CoA wild type enzyme, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 0.052
-
acetyl-CoA mutant enzyme E123D, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 0.64
-
4-aminosalicylic acid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 0.86
-
2-Aminofluorene mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 1.34
-
4-aminosalicylic acid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 5.8
-
2-Aminofluorene wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 14.55
-
isoniazid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 76.9
-
isoniazid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.5 33465
-
x * 33465, calculated from amino acid sequence Bacillus cereus
2.3.1.5 34000
-
x * 34000, SDS-PAGE Bacillus cereus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Bacillus cereus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.5 Ni-NTA column chromatography and Mono Q column chromatography Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + 2-aminofluorene
-
Bacillus cereus CoA + N-acetyl-2-aminofluorene
-
?
2.3.1.5 acetyl-CoA + 4-aminosalicylic acid
-
Bacillus cereus CoA + N-acetyl-4-aminosalicylate
-
?
2.3.1.5 acetyl-CoA + isoniazid
-
Bacillus cereus CoA + N-acetylisoniazid
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.5 ? x * 34000, SDS-PAGE Bacillus cereus
2.3.1.5 ? x * 33465, calculated from amino acid sequence Bacillus cereus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 NAT3
-
Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.5 14.3
-
acetyl-CoA mutant enzyme E123D, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 19.3
-
acetyl-CoA wild type enzyme, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 43.9
-
4-aminosalicylic acid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 44.1
-
2-Aminofluorene mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 56.6
-
4-aminosalicylic acid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 67.4
-
2-Aminofluorene wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 167.1
-
isoniazid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 289.3
-
isoniazid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.5 3.76
-
isoniazid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 11.5
-
isoniazid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 11.5
-
2-Aminofluorene wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 42.4
-
4-aminosalicylic acid wild type enzyme, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 51.3
-
2-Aminofluorene mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 68.4
-
4-aminosalicylic acid mutant enzyme E123D, apparent value, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 275
-
acetyl-CoA mutant enzyme E123D, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus
2.3.1.5 390
-
acetyl-CoA wild type enzyme, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C Bacillus cereus