Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Bacillus anthracis |
into the pET28a vector for expression in Escherichia coli BL21DE3 pLysS cells | Bacillus anthracis |
Protein Variants | Comment | Organism |
---|---|---|
C69A | BanatC inactive mutant, replacement of the catalytic cysteine residue | Bacillus anthracis |
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 |
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.084 | - |
2-Aminofluorene | apparent KM | Bacillus anthracis | |
0.084 | - |
2-Aminofluorene | isoenzyme BanatB | Bacillus anthracis | |
0.21 | - |
2-Aminofluorene | apparent KM | Bacillus anthracis | |
0.21 | - |
2-Aminofluorene | isoenzyme BanatC | Bacillus anthracis | |
0.228 | - |
5-Aminosalicylate | apparent KM | Bacillus anthracis | |
0.228 | - |
5-Aminosalicylate | isoenzyme BanatC | Bacillus anthracis | |
0.622 | - |
5-Aminosalicylate | apparent KM | Bacillus anthracis | |
0.622 | - |
5-Aminosalicylate | isoenzyme BanatB | Bacillus anthracis | |
0.662 | - |
sulfamethoxazole | apparent KM | Bacillus anthracis | |
0.662 | - |
sulfamethoxazole | isoenzyme BanatC | Bacillus anthracis | |
0.834 | - |
4-Aminosalicylate | apparent KM | Bacillus anthracis | |
0.834 | - |
4-Aminosalicylate | isoenzyme BanatC | Bacillus anthracis | |
0.849 | - |
hydralazine | apparent KM | Bacillus anthracis | |
0.849 | - |
hydralazine | isoenzyme BanatB | Bacillus anthracis | |
1.327 | - |
hydralazine | apparent KM | Bacillus anthracis | |
1.327 | - |
hydralazine | isoenzyme BanatC | Bacillus anthracis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
27000 | - |
His-tagged BanatA, determined by SDS-PAGE and Western blot analysis | Bacillus anthracis |
27000 | - |
SDS-PAGE isoenzyme BanatA | Bacillus anthracis |
31000 | - |
His-tagged BanatB, determined by SDS-PAGE and Western blot analysis | Bacillus anthracis |
31000 | - |
SDS-PAGE isoenzyme BanatB | Bacillus anthracis |
34000 | - |
His-tagged BanatC, determined by SDS-PAGE and Western blot analysis | Bacillus anthracis |
34000 | - |
SDS-PAGE, isoenzyme BanatC | Bacillus anthracis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | A0A0F7R932 | - |
- |
Bacillus anthracis | A0A0F7R932 | BanatA | - |
Bacillus anthracis | Q81PT0 | - |
- |
Bacillus anthracis | Q81PT0 | BanatB | - |
Bacillus anthracis | Q81R98 | - |
- |
Bacillus anthracis | Q81R98 | BanatC | - |
Purification (Comment) | Organism |
---|---|
using a HIS-Select nickel resin, CM Sephadex ion exchange chromatography | Bacillus anthracis |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
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 |
additional information | - |
no activity with substrates: isoniazid, 4-aminobenzoic acid, isoenzyme BanatC | Bacillus anthracis |
additional information | - |
substrate: sulfamethoxazolea, 4-aminobenzoic, 4-aminosalicylate, isoniazid acid no activity detected | Bacillus anthracis |
0.168 | - |
- |
Bacillus anthracis |
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 |
0.416 | - |
substrate: sulfamethoxazole, isoenzyme BanatC | Bacillus anthracis |
0.416 | - |
sulfamethoxazole | Bacillus anthracis |
0.603 | - |
2-aminofluorene | Bacillus anthracis |
0.603 | - |
substrate: 2-aminofluorenea | Bacillus anthracis |
0.969 | - |
hydralazine | Bacillus anthracis |
0.969 | - |
substrate: hydralazine | Bacillus anthracis |
1.36 | - |
5-aminosalicylate | Bacillus anthracis |
1.36 | - |
substrate: 5-aminosalicylate | Bacillus anthracis |
1.744 | - |
hydralazine | Bacillus anthracis |
1.744 | - |
substrate: hydralazine, isoenzyme BanatC | Bacillus anthracis |
3.109 | - |
4-aminosalicylate | Bacillus anthracis |
3.109 | - |
substrate: 4-aminosalicylate, isoenzyme BanatC | Bacillus anthracis |
3.679 | - |
5-aminosalicylate | Bacillus anthracis |
3.679 | - |
substrate: 5-aminosalicylate, isoenzyme BanatC | Bacillus anthracis |
5.852 | - |
2-aminofluorene | Bacillus anthracis |
5.852 | - |
substrate: 2-aminofluorene, isoenzyme BanatC | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + 2-aminofluorene | - |
Bacillus anthracis | CoA + N-acetyl-2-aminofluorene | - |
? | |
acetyl-CoA + 4-aminosalicylate | - |
Bacillus anthracis | CoA + N-acetyl-4-aminosalicylate | - |
? | |
acetyl-CoA + 5-aminosalicylate | - |
Bacillus anthracis | CoA + N-acetyl-5-aminosalicylate | - |
? | |
acetyl-CoA + hydralazine | - |
Bacillus anthracis | ? | - |
? | |
acetyl-CoA + hydralazine | - |
Bacillus anthracis | CoA + N-acetyl-hydralazine | - |
? | |
acetyl-CoA + sulfamethoxazole | - |
Bacillus anthracis | CoA + N-acetyl-sulfamethoxazole | - |
? | |
acetyl-CoA + sulfamethoxazole | - |
Bacillus anthracis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
arylamine N-acetyltransferase | - |
Bacillus anthracis |
BanatA | - |
Bacillus anthracis |
BanatB | - |
Bacillus anthracis |
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 |
BanatC | - |
Bacillus anthracis |
NAT | - |
Bacillus anthracis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bacillus anthracis |
37 | - |
activity assay | Bacillus anthracis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Bacillus anthracis |
7.5 | - |
activity assay | Bacillus anthracis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Bacillus anthracis |