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Literature summary extracted from

  • Pluvinage, B.; Dairou, J.; Possot, O.M.; Martins, M.; Fouet, A.; Dupret, J.M.; Rodrigues-Lima, F.
    Cloning and molecular characterization of three arylamine N-acetyltransferase genes from Bacillus anthracis: identification of unusual enzymatic properties and their contribution to sulfamethoxazole resistance (2007), Biochemistry, 46, 7069-7078.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.5 expressed in Escherichia coli as a His-tagged fusion protein Bacillus anthracis
2.3.1.5 into the pET28a vector for expression in Escherichia coli BL21DE3 pLysS cells Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.5 C69A BanatC inactive mutant, replacement of the catalytic cysteine residue Bacillus anthracis
2.3.1.5 C69A mutant devoid of NAT activity. Expression of the C69A mutant in Escherichia coli does not afford higher-than-normal resistance to sulfonamide antibiotic sulfamethoxazole in the recombinant bacteria Bacillus anthracis
2.3.1.5 additional information expression of BanatC in Escherichia coli affords higher-than-normal resistance to sulfonamide antibiotic sulfamethoxazole in the recombinant bacteria Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.5 0.084
-
 2-Aminofluorene apparent KM Bacillus anthracis
2.3.1.5 0.084
-
 2-Aminofluorene isoenzyme BanatB Bacillus anthracis
2.3.1.5 0.21
-
 2-Aminofluorene apparent KM Bacillus anthracis
2.3.1.5 0.21
-
 2-Aminofluorene isoenzyme BanatC Bacillus anthracis
2.3.1.5 0.228
-
 5-Aminosalicylate apparent KM Bacillus anthracis
2.3.1.5 0.228
-
 5-Aminosalicylate isoenzyme BanatC Bacillus anthracis
2.3.1.5 0.622
-
 5-Aminosalicylate apparent KM Bacillus anthracis
2.3.1.5 0.622
-
 5-Aminosalicylate isoenzyme BanatB Bacillus anthracis
2.3.1.5 0.662
-
 sulfamethoxazole apparent KM Bacillus anthracis
2.3.1.5 0.662
-
 sulfamethoxazole isoenzyme BanatC Bacillus anthracis
2.3.1.5 0.834
-
 4-Aminosalicylate apparent KM Bacillus anthracis
2.3.1.5 0.834
-
 4-Aminosalicylate isoenzyme BanatC Bacillus anthracis
2.3.1.5 0.849
-
 hydralazine apparent KM Bacillus anthracis
2.3.1.5 0.849
-
 hydralazine isoenzyme BanatB Bacillus anthracis
2.3.1.5 1.327
-
 hydralazine apparent KM Bacillus anthracis
2.3.1.5 1.327
-
 hydralazine isoenzyme BanatC Bacillus anthracis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.5 27000
-
 His-tagged BanatA, determined by SDS-PAGE and Western blot analysis Bacillus anthracis
2.3.1.5 27000
-
 SDS-PAGE isoenzyme BanatA Bacillus anthracis
2.3.1.5 31000
-
 His-tagged BanatB, determined by SDS-PAGE and Western blot analysis Bacillus anthracis
2.3.1.5 31000
-
 SDS-PAGE isoenzyme BanatB Bacillus anthracis
2.3.1.5 34000
-
 His-tagged BanatC, determined by SDS-PAGE and Western blot analysis Bacillus anthracis
2.3.1.5 34000
-
 SDS-PAGE, isoenzyme BanatC Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Bacillus anthracis A0A0F7R932
-
-
2.3.1.5 Bacillus anthracis A0A0F7R932 BanatA
-
2.3.1.5 Bacillus anthracis Q81PT0
-
-
2.3.1.5 Bacillus anthracis Q81PT0 BanatB
-
2.3.1.5 Bacillus anthracis Q81R98
-
-
2.3.1.5 Bacillus anthracis Q81R98 BanatC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.5 using a HIS-Select nickel resin, CM Sephadex ion exchange chromatography Bacillus anthracis
2.3.1.5 using HIS-select nickel resin and CM Sephadex ion exchange chromatography, in addition protein extracts from stationary phase cultures of Bacillus anthracis are preapred Bacillus anthracis

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
-
 BanatA is devoid of NAT or AcCoA/p-nitrophenyl acetate hydrolysis activities, suggesting that it may be a new bacterial NAT-like protein with unknown function Bacillus anthracis
2.3.1.5 additional information
-
 no activity with substrates: isoniazid, 4-aminobenzoic acid, isoenzyme BanatC Bacillus anthracis
2.3.1.5 additional information
-
 substrate: sulfamethoxazolea, 4-aminobenzoic, 4-aminosalicylate, isoniazid acid no activity detected Bacillus anthracis
2.3.1.5 0.168
-
-
 Bacillus anthracis
2.3.1.5 0.168
-
 enzymatic activity detected in the absence of an arylamine substrate: BanatB, but not BanatC, displays AcCoA and /or p-nitrophenyl acetate hydrolysis activity in the absence of an arylamine substrate Bacillus anthracis
2.3.1.5 0.416
-
 substrate: sulfamethoxazole, isoenzyme BanatC Bacillus anthracis
2.3.1.5 0.416
-
 sulfamethoxazole Bacillus anthracis
2.3.1.5 0.603
-
 2-aminofluorene Bacillus anthracis
2.3.1.5 0.603
-
 substrate: 2-aminofluorenea Bacillus anthracis
2.3.1.5 0.969
-
 hydralazine Bacillus anthracis
2.3.1.5 0.969
-
 substrate: hydralazine Bacillus anthracis
2.3.1.5 1.36
-
 5-aminosalicylate Bacillus anthracis
2.3.1.5 1.36
-
 substrate: 5-aminosalicylate Bacillus anthracis
2.3.1.5 1.744
-
 hydralazine Bacillus anthracis
2.3.1.5 1.744
-
 substrate: hydralazine, isoenzyme BanatC Bacillus anthracis
2.3.1.5 3.109
-
 4-aminosalicylate Bacillus anthracis
2.3.1.5 3.109
-
 substrate: 4-aminosalicylate, isoenzyme BanatC Bacillus anthracis
2.3.1.5 3.679
-
 5-aminosalicylate Bacillus anthracis
2.3.1.5 3.679
-
 substrate: 5-aminosalicylate, isoenzyme BanatC Bacillus anthracis
2.3.1.5 5.852
-
 2-aminofluorene Bacillus anthracis
2.3.1.5 5.852
-
 substrate: 2-aminofluorene, isoenzyme BanatC Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + 2-aminofluorene
-
 Bacillus anthracis CoA + N-acetyl-2-aminofluorene
-
 ?
2.3.1.5 acetyl-CoA + 4-aminosalicylate
-
 Bacillus anthracis CoA + N-acetyl-4-aminosalicylate
-
 ?
2.3.1.5 acetyl-CoA + 5-aminosalicylate
-
 Bacillus anthracis CoA + N-acetyl-5-aminosalicylate
-
 ?
2.3.1.5 acetyl-CoA + hydralazine
-
 Bacillus anthracis ?
-
 ?
2.3.1.5 acetyl-CoA + hydralazine
-
 Bacillus anthracis CoA + N-acetyl-hydralazine
-
 ?
2.3.1.5 acetyl-CoA + sulfamethoxazole
-
 Bacillus anthracis CoA + N-acetyl-sulfamethoxazole
-
 ?
2.3.1.5 acetyl-CoA + sulfamethoxazole
-
 Bacillus anthracis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 arylamine N-acetyltransferase
-
 Bacillus anthracis
2.3.1.5 BanatA
-
 Bacillus anthracis
2.3.1.5 BanatB
-
 Bacillus anthracis
2.3.1.5 BanatB in contrast to BanatA or BanatC, BanatB also has acetyl-CoA and p-nitrophenyl acetate hydrolysis activity in the absence of arylamine substrates, indicating that it may act also as an AcCoA hydrolase Bacillus anthracis
2.3.1.5 BanatC
-
 Bacillus anthracis
2.3.1.5 NAT
-
 Bacillus anthracis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.5 37
-
 assay at Bacillus anthracis
2.3.1.5 37
-
 activity assay Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.5 7.5
-
 assay at Bacillus anthracis
2.3.1.5 7.5
-
 activity assay Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.5 acetyl-CoA
-
 Bacillus anthracis