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Information on EC 2.3.1.118 - N-hydroxyarylamine O-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.118
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.118 N-hydroxyarylamine O-acetyltransferase
IUBMB Comments
The enzyme from liver, but not that from bacteria, can also catalyse N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.118
- typhimurium
- n-acetyltransferase
-
nitroarenes
- 4-aminobiphenyl
-
glu-p-1
-
tester
- 1-nitropyrene
-
1,8-dinitropyrene
-
plant-activated
- 2-aminoanthracene
- benzidine
-
polyguanylic
-
arylhydroxamic
- beta-naphthylamine
-
2-amino-6-methyldipyrido1,2-a:3',2'-dimidazole
-
3-hydroxyamino-1-methyl-5h-pyrido4,3-bindole
-
genotype-independent
-
nitroaromatics
- 2-nitrofluorene
-
promutagens
- m-phenylenediamine
-
o-acetylation
- pentachlorophenol
showSynonyms
n-hydroxyarylamine o-acetyltransferase, nhoa1, acetyl-coa:n-hydroxyarylamine o-acetyltransferase, nhoa2, n-arylamine acetyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, N-hydroxyarylamine O-
-
-
-
-
arylamine N-acetyltransferase
-
-
-
-
arylhydroxamate N,O-acetyltransferase
-
-
-
-
N-hydroxy-2-aminofluorene-O-acetyltransferase
-
-
-
-
N-hydroxyarylamine O-acetyltransferase
NhoA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-hydroxyarylamine O-acetyltransferase
The enzyme from liver, but not that from bacteria, can also catalyse N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.
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CAS REGISTRY NUMBER
COMMENTARY
100984-92-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 2-aminofluorene
CoA + 2-acetylaminofluorene
-
Substrates: N-acetyltransferase activity
Products: -
Products: -
?
acetyl-CoA + 2-aminofluorene
CoA + N-acetyl-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
acetyl-CoA + 3-amino-4-hydroxyphenylarsonic acid
CoA + N-acetyl-3-amino-4-hydroxyphenylarsonic acid
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-hydroxyamino-1-methyl-pyrido[4,3-b]-indole
CoA + N-acetoxy-amino-1-methyl-pyrido[4,3-b]-indole
acetyl-CoA + 4-aminoveratrole
CoA + N-acetyl-4-aminoveratrole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 4-anisidine
CoA + N-acetyl-4-anisidine
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 4-iodoaniline
CoA + N-acetyl-4-iodoaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + aniline
CoA + N-acetylaniline
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + isoniazid
CoA + N-acetyl-isoniazid
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + m-aminophenol
CoA + N-acetyl-m-aminophenol
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-acetylaminofluorene
?
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-3,2'-dimethyl-4-aminobiphenyl
CoA + N-acetoxy-3,2'-dimethyl-4-aminobiphenyl
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + o-aminophenol
CoA + N-acetyl-o-aminophenol
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + o-anisidine
CoA + N-acetyl-o-anisidine
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + p-aminobenzoic acid
CoA + N-acetyl-p-aminobenzoic acid
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + p-aminophenol
CoA + N-acetyl-p-aminophenol
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + p-aminotoluene
CoA + N-acetyl-p-aminotoluene
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + p-anisidine
CoA + N-acetyl-p-anisidine
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
butyryl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-(butyryloxy)-6-methylpyrido[3',2':4,5]imidazo[1,2-a]pyridin-2-amine
hexanoyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-hexanoyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
malonyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-malonyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
p-aminobenzoic acid + acetyl-CoA
N-acetyl-p-aminobenzoic acid + CoA
-
Substrates: -
Products: -
Products: -
?
propionyl-CoA + 2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-propionyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
sulfadiazine + acetyl-CoA
N-acetyl-sulfadiazine + CoA
-
Substrates: -
Products: -
Products: -
?
sulfamethazine + acetyl-CoA
N-acetyl-sulfamethazine + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: N-hydroxy-2-acetylaminofluorene cannot replace acetyl-CoA
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: N-hydroxy-2-acetylaminofluorene cannot replace acetyl-CoA
Products: -
Products: -
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-hydroxyamino-1-methyl-pyrido[4,3-b]-indole
CoA + N-acetoxy-amino-1-methyl-pyrido[4,3-b]-indole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-hydroxyamino-1-methyl-pyrido[4,3-b]-indole
CoA + N-acetoxy-amino-1-methyl-pyrido[4,3-b]-indole
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: unknown endogenous substrate in bacteria
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetoxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetoxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetoxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetoxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetyloxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetyloxy-2-aminofluorene
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-4-aminobiphenyl
CoA + N-acetoxy-4-aminobiphenyl
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-hydroxy-4-aminobiphenyl
CoA + N-acetoxy-4-aminobiphenyl
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + o-aminobenzoic acid
CoA + N-acetyl-o-aminobenzoic acid
-
Substrates: N-acetyltransferase activity, ping-pong bi bi mechanism
Products: -
Products: -
?
acetyl-CoA + o-aminobenzoic acid
CoA + N-acetyl-o-aminobenzoic acid
-
Substrates: o-aminobenzoic acid is intermediate in the synthesis of tryptophane in E. coli
Products: -
Products: -
?
butyryl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-(butyryloxy)-6-methylpyrido[3',2':4,5]imidazo[1,2-a]pyridin-2-amine
-
Substrates: 11% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
butyryl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-(butyryloxy)-6-methylpyrido[3',2':4,5]imidazo[1,2-a]pyridin-2-amine
-
Substrates: 11% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
hexanoyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-hexanoyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 1.3% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
hexanoyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-hexanoyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 1.3% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
malonyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-malonyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 19% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
malonyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-malonyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 19% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
propionyl-CoA + 2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-propionyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 89% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
propionyl-CoA + 2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-propionyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
Substrates: 89% of the activity compared to acetyl-CoA as acyl donor
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates of either isoform NhoA1 or NhoA2: 4-amino-phenylarsonic acid, 2-amino-phenylarsonic acid, and 4-carbamoylamino-phenylarsonic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is deacetylated by CobB
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is deacetylated by CobB
Products: -
Products: -
?
additional information
?
-
-
Substrates: the N-acetoxyarylamine products form covalent adducts with cellular macromolecules, e.g. tRNA
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + o-aminobenzoic acid
CoA + N-acetyl-o-aminobenzoic acid
-
Substrates: o-aminobenzoic acid is intermediate in the synthesis of tryptophane in E. coli
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: involved in mutagenic, metabolic activation of carcinogenic arylamines to form DNA-binding species
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: the enzyme from liver, but not from bacteria, can also catalyse acetylation of arylamines and N,O-acetylation of arylhydroxamates
Products: -
Products: -
?
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
-
Substrates: unknown endogenous substrate in bacteria
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
-
-
N-ethylmaleimide
-
1 mM, 65% inhibition of isoform NhoA1, 45% inhibition of isoform NhoA2
paraoxon
-
0.1 mM, 23.5% inhibition of isoform NhoA1, 14% inhibition of isoform NhoA2
additional information
-
inhibition by salicylic acid and N-ethylmaleimide is non competitive with acetyl-CoA and competitive with o-aminobenzoic acid
-
additional information
-
thiolactomycin does not inhibit enzyme from Syrian golden hamster
-
additional information
-
no inhibition by 2,6-dichloro-4-nitrophenol, chloramphenicol, hydroxylamine; no inhibition by paraoxon
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.151
3-amino-4-hydroxyphenylarsonic acid
-
isoform NhoA1, pH 7.4, 30°C
0.428
3-amino-4-hydroxyphenylarsonic acid
-
isoform NhoA2, pH 7.4, 30°C
0.0033
acetyl-CoA
-
reaction with O-acetyl transfer to 2-hydroxyamino-6-methyldipyrido[1,2-alpha: 3',2'-d]imidazole as substrate
0.0033
acetyl-CoA
-
fluorometric method
0.01
acetyl-CoA
-
reaction with 2-hydroxy-amino-6-methyldipyrido[1,2-alpha: 3',2'-d]imidazole as substrate
0.37
acetyl-CoA
-
reaction of O-acetyl transfer to 2-hydroxyamino-6-methyldipyrido[1,2-alpha: 3',2'-d]imidazole
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
-
N-acetylation of p-aminobenzoic acid
0.126
-
2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
0.517
-
N-acetylation of 2-aminofluorene
0.82
-
2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
1.31
-
2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
additional information
additional information
-
activity in different tissues might be related to carcinogenesis
additional information
-
specific activities in different tissues for three hamster phenotypes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
fast and slow acetylating phenotypes, may be identical with EC 2.3.1.5
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high polymorphism, two isozymes with different chromatographic properties and kinetic constants
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
deletion of of isoforms NhoA1 and NhoA2 decreases 3-amino-4-hydroxyphenylarsonic acid acetylation activity by 97 and 14%, respectively, the double mutant loses the acetylation activity completely. Deletion of isoform NhoA1 increases the release of inorganic As(III) and As(V) from3 -amino-4-hydroxyphenylarsonic acid or roxarsone
Show AA Sequence and Transmembrane Helices (594 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32180
-
calculated from nucleotide sequence
33000
33570
-
electrospray mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sodium potassium tartrate and X-ray diffraction
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K214R
-
the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
K214R/K281R
-
the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
K281R
-
the mutant exhibits an about 12% decrease in enzyme activity compared to the wild type enzyme
K214R
-
the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
-
K214R/K281R
-
the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
-
K281R
-
the mutant exhibits an about 12% decrease in enzyme activity compared to the wild type enzyme
-
A69C
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
A69R
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
A69C
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69R
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69C
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69R
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, elution buffer, 1 month, 89% residual activity for isoform NhoA1, 95% residual activity for isoform NhoA2, respectively
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange chromatography, gel filtration, immunoaffinity chromatograpy with protein A Sepharose columns
-
copurifies with arylamine acetyltransferase and arylhydroxamic acid N,O-acetyltransferase
-
partial, by ammonium sulfate precipitation, DEAE-cellulose and Sephadex-G150 column chromatography
-
purification by ammonium sulfate followed by DEAE cellulose, gel filtration on GCL-2000 and HPKB-hydroxyapatite chromatography
-
single step immobilized metal ion chromatography
-
streptomycin, ammonium sulfate precipitation, DEAE Cellulose, Sephadex G-150 chromatograpy
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
16 recombinant NAT2 allozymes expressed in Escherichia coli JM105 expression system
-
cloned and expression of wild type and two mutant enzymes in Escherichia coli XL-1-Blue maxi cells, plasmid pYG122
-
construction of 2 oat-null mutants specifically disrupted by replacing the oat gene with the chloramphenicol resistance gene using the preligation method
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saito, K.; Shinohara, A.; Kamataki, T.; Kato, R.
N-Hydroxyarylamine O-acetyltransferase in hamster liver: identity with arylhydroxamic acid N,O-acetyltransferase and arylamine N-acetyltransferase
J. Biochem.
99
1689-1697
1986
Mesocricetus auratus
brenda
Saito, K.; Shinohara, A.; Kamataki, T.; Kato, R.
Metabolic activation of mutagenic N-hydroxyarylamines by O-acetyltransferase in Salmonella typhimurium TA98
Arch. Biochem. Biophys.
239
286-295
1985
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA98
brenda
Watanabe, M.; Sofuni, T.; Nohmi, T.
Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium. Sequence similarity at the amino acid level suggests a common catalytic mechanism of acetyltransferase for S. typhimurium and higher organisms
J. Biol. Chem.
267
8429-8436
1992
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA 1538, Salmonella enterica subsp. enterica serovar Typhimurium TA98
brenda
Saito, K.; Shinohara, A.; Kamataki, T.; Kato, R.
A new assay for N-hydroxyarylamine O-acetyltransferase: reduction of N-hydroxyarylamines through N-acetoxyarylamines
Anal. Biochem.
152
226-231
1986
Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA98
brenda
Glowinski, I.B.; Weber, W.W.; Fysh, J.M.; Vaught, J.B.; King, C.M.
Evidence that arylhydroxamic acid N,O-acyltransferase and the genetically polymorphic N-acetyltransferase are properties of the same enzyme in rabbit liver
J. Biol. Chem.
255
7883-7890
1980
Oryctolagus cuniculus
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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
Biochim. Biophys. Acta
1475
10-16
2000
Escherichia coli
brenda
Hein, D.; Doll, M.; Rustan, T.; Ferguson, R.
Metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by 16 recombinant human NAT2 allozymes: effects of 7 specific NAT2 nucleic acid substitutions
Cancer Res.
55
3531-3536
1995
Homo sapiens
brenda
Sinclair, J.; Delgoda, R.; Noble, M.; Jarmin, S.; Goh, N.; Sim, E.
Purification, characterization and crystallization of an N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium
Protein Expr. Purif.
12
371-380
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Land, S.; Zukowski, K.; Lee, M.; Wang, Ch.; King, Ch.
Purification and characterization of a rat hepatic acetyltransferase that can metabolize aromatic amine derivatives
Carcinogenesis
14
1441-1449
1993
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Espinosa-Aguirre, J.; Yamada, M.; Maiso, K.; Watanabe, M.; Sofuni, T.; Nukuri, T.
New O-acetyltransferase deficient ames Salmonella strains generated by specific gene disruption
Mutat. Res.
439
159-169
1999
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA100, Salmonella enterica subsp. enterica serovar Typhimurium TA98
brenda
Hein, D.W.
Acetylator genotype and arylamine-induced carcinogenesis
Biochim. Biophys. Acta
948
37-66
1988
Homo sapiens, Mesocricetus auratus, Mus musculus, Mus musculus C57/BL6J, Oryctolagus cuniculus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Winter, H.R.; Unadkat, J.D.
Identification of cytochrome P450 and arylamine N-acetyltransferase isoforms involved in sulfadiazine metabolism
Drug Metab. Dispos.
33
969-976
2005
Homo sapiens
brenda
Summerscales, J.E.; Josephy, P.D.
Human acetyl CoA:arylamine N-acetyltransferase variants generated by random mutagenesis
Mol. Pharmacol.
65
220-226
2004
Homo sapiens
brenda
Zhang, Q.F.; Gu, J.; Gong, P.; Wang, X.D.; Tu, S.; Bi, L.J.; Yu, Z.N.; Zhang, Z.P.; Cui, Z.Q.; Wei, H.P.; Tao, S.C.; Zhang, X.E.; Deng, J.Y.
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase
FEBS J.
280
1966-1979
2013
Escherichia coli
brenda
Huang, K.; Gao, F.; Le, X.C.; Zhao, F.J.
N-Hydroxyarylamine O-acetyltransferases catalyze acetylation of 3-amino-4-hydroxyphenylarsonic acid in the 4-hydroxy-3-nitrobenzenearsonic acid transformation pathway of Enterobacter sp. strain CZ-1
Appl. Environ. Microbiol.
86
e02050
2020
Enterobacter sp. CZ-1
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