GO:0046990 N-hydroxyarylamine O-acetyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0046990 N-hydroxyarylamine O-acetyltransferase activity catalyzes the acetyl-CoA-dependent O-acetylation of N-hydroxyarylamines to N-acetoxyarylamines.
• The enzyme is a member of the arylamine N-acetyltransferase (NAT) family and shares a common catalytic mechanism involving a catalytic cysteine residue [1,8].
• In bacteria such as Salmonella typhimurium and Escherichia coli, this activity is encoded by the nhoA gene and is involved in the activation of arylamine carcinogens [1,6].
• In mammals, hepatic and intestinal N-hydroxyarylamine O-acetyltransferase activity co-purifies with polymorphic arylamine N-acetyltransferase, linking it to acetylator genotype-dependent metabolism [2,5,7].
• The enzyme is relevant to chemical carcinogenesis because N-acetoxyarylamines can form DNA adducts, and to bioremediation because it participates in the transformation of aromatic arsenicals.
• Studying GO:0046990 requires biochemical assays, mutagenesis, and CRISPR-based models to dissect its role in drug metabolism, toxicity, and microbial pathways [4,8].
Description
N-hydroxyarylamine O-acetyltransferase activity (GO:0046990) is a molecular function defined as the catalysis of the reaction: acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine. This activity is central to the metabolic activation of arylamine and heterocyclic amine carcinogens, converting N-hydroxyarylamine intermediates into highly reactive N-acetoxyarylamines that can form DNA adducts [1,2]. The enzyme belongs to the arylamine N-acetyltransferase (NAT) family, which is characterized by a conserved catalytic cysteine residue and a common acetylation mechanism [1,8]. In bacteria, the activity was first characterized in Salmonella typhimurium, where it is encoded by the nhoA gene and contributes to the mutagenicity of arylamines [1,8]. In mammals, N-hydroxyarylamine O-acetyltransferase activity is expressed in liver, intestine, and colon, and co-purifies with polymorphic arylamine N-acetyltransferase, indicating that the same enzyme can catalyze both N-acetylation and O-acetylation reactions [2,5,7]. This dual activity underlies interindividual differences in susceptibility to arylamine-induced cancers [5,7]. Beyond toxicology, recent work has shown that N-hydroxyarylamine O-acetyltransferases can acetylate 3-amino-4-hydroxyphenylarsonic acid in the transformation pathway of 4-hydroxy-3-nitrobenzenearsonic acid in Enterobacter sp. strain CZ-1, expanding the known substrate range to environmental arsenicals. Understanding GO:0046990 is therefore important for researchers in chemical carcinogenesis, drug metabolism, and microbial biotechnology.
N-hydroxyarylamine O-acetyltransferase activity At A Glance
| GO ID | GO:0046990 |
|---|---|
| GO term | N-hydroxyarylamine O-acetyltransferase activity |
| Ontology | molecular_function |
| Synonym | acetyl-CoA:N-hydroxyarylamine O-acetyltransferase activity; arylhydroxamate N,O-acetyltransferase activity; N-hydroxy-2-aminofluorene-O-acetyltransferase activity |
| Definition | Catalysis of the reaction: acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine. |
| Major function | O-acetylation of N-hydroxyarylamines using acetyl-CoA as the acetyl donor, producing N-acetoxyarylamines and CoA. |
| Catalytic residue | A conserved cysteine residue (e.g., Cys69 in Salmonella typhimurium) is essential for catalysis. |
| Representative enzymes | Bacterial NhoA (Salmonella typhimurium, Escherichia coli) and mammalian arylamine N-acetyltransferases (NAT1, NAT2) [1,2,6]. |
| Pathological relevance | Implicated in the metabolic activation of arylamine carcinogens and in the biotransformation of aromatic arsenicals [1,3]. |
What Is GO:0046990?
GO:0046990 N-hydroxyarylamine O-acetyltransferase activity is defined by QuickGO as the catalysis of the reaction: acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine. In other words, the enzyme transfers an acetyl group from acetyl-CoA to the oxygen atom of an N-hydroxyarylamine, producing an N-acetoxyarylamine and coenzyme A. This O-acetylation reaction is distinct from N-acetylation, which targets the nitrogen atom of arylamines. The activity is synonymous with acetyl-CoA:N-hydroxyarylamine O-acetyltransferase activity, arylhydroxamate N,O-acetyltransferase activity, and N-hydroxy-2-aminofluorene-O-acetyltransferase activity, reflecting its ability to act on a range of N-hydroxyarylamine and arylhydroxamate substrates [1,2].
Why Is N-hydroxyarylamine O-acetyltransferase activity Important in Cell Biology?
GO:0046990 is important because it represents a key step in the bioactivation of arylamine and heterocyclic amine carcinogens, converting relatively stable N-hydroxyarylamine metabolites into highly reactive N-acetoxyarylamines that can bind DNA and initiate mutagenesis and carcinogenesis [1,2]. The activity is also a marker of the polymorphic acetylation pathway in humans and animal models, where interindividual differences in N-acetylation and O-acetylation capacity influence susceptibility to bladder, colon, and other cancers [5,7]. In bacteria, the enzyme contributes to the mutagenicity of environmental arylamines and to the degradation or transformation of aromatic compounds, including arsenicals [1,3]. Thus, understanding GO:0046990 has implications for toxicology, cancer epidemiology, drug metabolism, and bioremediation.
• Metabolic activation of arylamine carcinogens: converts N-hydroxyarylamines to DNA-reactive N-acetoxyarylamines [1,2].
• Acetylator genotype-dependent expression: activity co-purifies with polymorphic arylamine N-acetyltransferase in liver, intestine, and colon [5,7].
• Bacterial mutagenicity: the nhoA gene product in Salmonella typhimurium and Escherichia coli activates arylamines to mutagens [1,6].
• Common catalytic mechanism: shares a conserved cysteine-dependent mechanism with other arylamine acetyltransferases [1,8].
• Environmental biotechnology: catalyzes acetylation of 3-amino-4-hydroxyphenylarsonic acid in the transformation of aromatic arsenicals.
• Post-translational regulation: reversibly acetylated lysine residues modulate the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.
• Species differences: hepatic and intestinal activities differ between rapid and slow acetylator inbred hamsters, providing models for human polymorphism [5,7].
• Substrate diversity: acts on N-hydroxy-2-aminofluorene and other arylhydroxamates, linking it to heterocyclic amine toxicity.
What Happens During N-hydroxyarylamine O-acetyltransferase activity?
Substrate binding and acetyl-CoA orientation
In simple terms: The enzyme grabs an N-hydroxyarylamine and an acetyl-CoA molecule and positions them for reaction.
The reaction begins with binding of the N-hydroxyarylamine substrate and the acetyl donor, acetyl-CoA, to the enzyme active site. In Salmonella typhimurium N-hydroxyarylamine O-acetyltransferase, the active site contains a catalytic cysteine residue (Cys69) that is essential for catalysis. Sequence similarity among arylamine acetyltransferases suggests a common catalytic mechanism in which the enzyme forms an acetyl-enzyme intermediate before transferring the acetyl group to the substrate.
Acetyl transfer and formation of N-acetoxyarylamine
In simple terms: The acetyl group is transferred from acetyl-CoA to the N-hydroxyarylamine, making a reactive N-acetoxyarylamine.
Following substrate binding, the acetyl group from acetyl-CoA is transferred to the oxygen atom of the N-hydroxyarylamine, yielding an N-acetoxyarylamine and coenzyme A. This O-acetylation reaction is the defining catalytic event of GO:0046990. The product, N-acetoxyarylamine, is electrophilic and can react with nucleophilic sites in DNA, which is the basis for its mutagenic and carcinogenic potential [1,2].
Enzyme acetylation and catalytic cycle
In simple terms: The enzyme itself can be temporarily acetylated, and this modification affects how well it works.
The catalytic cycle involves transient acetylation of the enzyme. In Escherichia coli N-hydroxyarylamine O-acetyltransferase, reversibly acetylated lysine residues play important roles in enzymatic activity, indicating that post-translational acetylation can modulate the catalytic cycle. The conserved cysteine residue is thought to form a covalent acetyl-enzyme intermediate, which then transfers the acetyl group to the N-hydroxyarylamine substrate.
Substrate specificity and product release
In simple terms: The enzyme can act on different N-hydroxyarylamines, and the products are released to participate in downstream reactions.
N-hydroxyarylamine O-acetyltransferase activity is not limited to a single substrate. It can acetylate N-hydroxy-2-aminofluorene and other arylhydroxamates, as reflected in the synonym N-hydroxy-2-aminofluorene-O-acetyltransferase activity. In Enterobacter sp. strain CZ-1, the enzyme catalyzes acetylation of 3-amino-4-hydroxyphenylarsonic acid in the 4-hydroxy-3-nitrobenzenearsonic acid transformation pathway, demonstrating a broader substrate range that includes aromatic arsenicals. After catalysis, the N-acetoxyarylamine and CoA products are released, and the enzyme returns to its resting state.
Key Genes Involved in GO:0046990 N-hydroxyarylamine O-acetyltransferase activity
The following genes and proteins are directly associated with N-hydroxyarylamine O-acetyltransferase activity (GO:0046990) based on published biochemical and genetic studies.
| Gene | Major Role | Research Relevance |
|---|---|---|
| nhoA (Salmonella typhimurium) | Encodes N-hydroxyarylamine O-acetyltransferase; catalyzes O-acetylation of N-hydroxyarylamines | Model enzyme for the common catalytic mechanism of arylamine acetyltransferases [1,8] |
| nhoA (Escherichia coli) | Encodes an N-hydroxyarylamine O-acetyltransferase with broad substrate specificity | Biochemical characterization and regulation by lysine acetylation [4,6] |
| NAT1 (mammalian) | Arylamine N-acetyltransferase 1; contributes to N-hydroxyarylamine O-acetyltransferase activity | Polymorphic enzyme linked to cancer susceptibility [2,5] |
| NAT2 (mammalian) | Arylamine N-acetyltransferase 2; co-purifies with N-hydroxyarylamine O-acetyltransferase activity | Acetylator genotype-dependent expression in liver and intestine [5,7] |
| NAT (hamster liver) | Hepatic polymorphic arylamine N-acetyltransferase with O-acetyltransferase activity | Identity with N-hydroxyarylamine O-acetyltransferase demonstrated by purification [2,5] |
| NAT (hamster intestine) | Intestinal arylamine N-acetyltransferase and N-hydroxyarylamine O-acetyltransferase | Acetylator genotype-dependent expression in intestine and colon |
| Enterobacter sp. CZ-1 NhoA-like | Acetylates 3-amino-4-hydroxyphenylarsonic acid in aromatic arsenical transformation | Environmental biotechnology and arsenical detoxification |
| Cys69 (Salmonella typhimurium NhoA) | Catalytic cysteine residue essential for O-acetyltransferase activity | Mechanistic studies of the acetyl-enzyme intermediate |
| Lysine residues (E. coli NhoA) | Reversible acetylation sites that modulate enzymatic activity | Post-translational regulation of O-acetyltransferase |
| Acetyl-CoA | Acetyl donor for the O-acetylation reaction | Central cofactor in the reaction catalyzed by GO:0046990 |
| N-hydroxy-2-aminofluorene | Model N-hydroxyarylamine substrate | Substrate specificity and carcinogen activation studies |
| 3-Amino-4-hydroxyphenylarsonic acid | Substrate for N-hydroxyarylamine O-acetyltransferase in Enterobacter sp. CZ-1 | Arsenical biotransformation pathway |
| Arylhydroxamic acid | Substrate for N,O-acetyltransferase activity | Historical synonym and substrate range |
| CoA | Product of the O-acetylation reaction | Reaction stoichiometry and enzyme assays |
| N-acetoxyarylamine | Reactive product that can form DNA adducts | Carcinogenesis and mutagenesis studies [1,2] |
How Is N-hydroxyarylamine O-acetyltransferase activity Regulated?
N-hydroxyarylamine O-acetyltransferase activity is regulated at multiple levels. In Escherichia coli, reversible acetylation of lysine residues on the enzyme modulates its enzymatic activity, providing a post-translational mechanism for regulation. In mammals, expression of the activity is acetylator genotype-dependent: rapid and slow acetylator inbred hamsters show different levels of arylamine N-acetyltransferase and N-hydroxyarylamine O-acetyltransferase in liver, intestine, and colon, indicating genetic control of enzyme expression [5,7]. The activity co-purifies with polymorphic arylamine N-acetyltransferase, suggesting that the same gene product is responsible for both N-acetylation and O-acetylation, and that regulation of NAT gene expression directly affects O-acetyltransferase capacity [2,5].
N-hydroxyarylamine O-acetyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| NAT1/NAT2 | Bladder and colorectal cancer susceptibility; arylamine carcinogen activation | Knockout or point-mutation cell lines (e.g., HepG2, Caco-2) with NAT1/NAT2 edited |
| nhoA (Salmonella typhimurium) | Bacterial mutagenicity of arylamines | Salmonella typhimurium strains with nhoA knockout or point mutations |
| nhoA (Escherichia coli) | Regulation of O-acetyltransferase by lysine acetylation | E. coli strains with lysine-to-arginine point mutations in nhoA |
| Enterobacter sp. CZ-1 NhoA-like | Aromatic arsenical transformation and detoxification | Enterobacter sp. CZ-1 with nhoA-like gene knockout or overexpression |
| Hamster NAT (rapid/slow acetylator) | Acetylator genotype-dependent cancer susceptibility | Inbred hamster models with rapid or slow acetylator genotypes |
Arylamine-induced carcinogenesis
N-hydroxyarylamine O-acetyltransferase activity is directly implicated in the metabolic activation of arylamine and heterocyclic amine carcinogens. By converting N-hydroxyarylamines to N-acetoxyarylamines, the enzyme generates electrophilic species that can form DNA adducts and induce mutations [1,2]. This pathway is a key mechanism by which compounds such as N-hydroxy-2-aminofluorene exert their mutagenic effects. In animal models, acetylator genotype-dependent expression of the activity in liver, intestine, and colon correlates with differences in susceptibility to arylamine-induced tumors [5,7].
Bladder and colorectal cancer susceptibility
Polymorphic arylamine N-acetyltransferase, which co-purifies with N-hydroxyarylamine O-acetyltransferase activity, has been linked to interindividual differences in bladder and colorectal cancer risk following exposure to arylamine carcinogens [5,7]. Rapid acetylator phenotypes may have higher O-acetylation capacity in target tissues, leading to increased DNA adduct formation and cancer initiation. The identity of the O-acetyltransferase with polymorphic NAT provides a mechanistic basis for these epidemiological associations [2,5].
Environmental arsenical transformation
In Enterobacter sp. strain CZ-1, N-hydroxyarylamine O-acetyltransferase catalyzes the acetylation of 3-amino-4-hydroxyphenylarsonic acid in the 4-hydroxy-3-nitrobenzenearsonic acid transformation pathway. This activity is relevant to the environmental fate of aromatic arsenicals and may influence arsenic toxicity and bioremediation strategies.
From N-hydroxyarylamine O-acetyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of N-hydroxyarylamine O-acetyltransferase activity reduce arylamine-induced mutagenesis? | Knockout of nhoA in Salmonella typhimurium or E. coli |
| Which cysteine residue is essential for catalysis? | Point mutation (Cys-to-Ala) in nhoA followed by biochemical assay |
| Does lysine acetylation regulate enzyme activity? | Point mutation of lysine residues to arginine or glutamine in E. coli nhoA |
| Can the enzyme act on aromatic arsenicals? | Overexpression of Enterobacter sp. CZ-1 nhoA-like gene in a heterologous host |
| What is the effect of NAT1/NAT2 polymorphism on O-acetylation capacity? | Knock-in of rapid or slow acetylator alleles in mammalian cell lines |
| Can we track enzyme localization and expression? | Tagged knock-in of nhoA or NAT with fluorescent or epitope tags |
How to Study the N-hydroxyarylamine O-acetyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Enzyme activity assay with acetyl-CoA and N-hydroxyarylamine | O-acetylation rate and substrate specificity | Biochemical characterization of purified enzyme [1,2] |
| HPLC or LC-MS | Formation of N-acetoxyarylamine or CoA | Product identification and quantification [1,3] |
| Site-directed mutagenesis | Role of specific residues (e.g., Cys69, lysines) in catalysis | Mechanistic studies [4,8] |
| Western blotting | Protein expression levels | Tissue-specific expression and acetylator genotype [5,7] |
| Genotyping (PCR-RFLP, sequencing) | NAT1/NAT2 polymorphisms | Association with cancer susceptibility |
| Bacterial mutagenicity assay (Ames test) | Mutagenic potential of arylamines | Role of nhoA in activation |
| Microbial transformation assays | Acetylation of aromatic arsenicals | Bioremediation and environmental fate |
| Recombinant protein expression and purification | Enzyme purity and kinetic parameters | Structural and kinetic studies |
Biochemical enzyme assays
N-hydroxyarylamine O-acetyltransferase activity is typically measured by incubating the enzyme with acetyl-CoA and an N-hydroxyarylamine substrate, then quantifying the formation of N-acetoxyarylamine or CoA. Such assays were used to purify and characterize the enzyme from hamster liver, Salmonella typhimurium, and Escherichia coli [1,2,6]. High-performance liquid chromatography (HPLC) or spectrophotometric methods can monitor substrate consumption or product formation.
Mutagenesis and site-directed mutagenesis
Site-directed mutagenesis is used to probe the catalytic mechanism. For example, mutation of Cys69 in Salmonella typhimurium N-hydroxyarylamine O-acetyltransferase abolishes activity, demonstrating its essential role. Similarly, lysine-to-arginine substitutions in Escherichia coli N-hydroxyarylamine O-acetyltransferase reveal the importance of reversible acetylation for enzymatic activity.
Gene expression and polymorphism analysis
Acetylator genotype-dependent expression can be studied by measuring mRNA and protein levels of NAT genes in different tissues. Purification of hepatic polymorphic arylamine N-acetyltransferase from rapid and slow acetylator hamsters demonstrated identity with N-hydroxyarylamine O-acetyltransferase and provided a model for human polymorphism [5,7]. Genotyping of NAT1 and NAT2 alleles in human populations is used to link genotype to enzyme activity and cancer risk.
Microbial transformation and bioremediation studies
In environmental microbiology, the activity can be studied by growing Enterobacter sp. strain CZ-1 in the presence of aromatic arsenicals and monitoring the formation of acetylated products. This approach revealed that N-hydroxyarylamine O-acetyltransferases catalyze acetylation of 3-amino-4-hydroxyphenylarsonic acid in the 4-hydroxy-3-nitrobenzenearsonic acid transformation pathway.
How CRISPR Can Be Used to Study GO:0046990 N-hydroxyarylamine O-acetyltransferase activity
Knockout
CRISPR knockout of nhoA in Salmonella typhimurium or Escherichia coli can be used to eliminate N-hydroxyarylamine O-acetyltransferase activity and test its contribution to arylamine mutagenicity or arsenical transformation [1,3]. In mammalian cells, knockout of NAT1 or NAT2 can reduce O-acetylation capacity and alter sensitivity to arylamine-induced DNA damage [5,7].
Point Mutation
CRISPR-mediated point mutations can introduce specific amino acid substitutions, such as Cys69Ala in Salmonella typhimurium nhoA, to dissect the catalytic mechanism. Similarly, lysine-to-arginine mutations in Escherichia coli nhoA can test the role of reversible acetylation in enzyme regulation.
Knock-in
Knock-in of rapid or slow acetylator alleles of NAT1 or NAT2 into a defined cell line can model human acetylator polymorphism and its effect on N-hydroxyarylamine O-acetyltransferase activity [5,7]. Tagged knock-in of nhoA or NAT with fluorescent or epitope tags enables localization and interaction studies.
Overexpression
Overexpression of nhoA or NAT genes in bacterial or mammalian cells can increase O-acetylation capacity, facilitating biochemical purification and substrate specificity studies. In Enterobacter sp. CZ-1, overexpression of the nhoA-like gene can enhance the transformation of aromatic arsenicals.
How EDITGENE Supports N-hydroxyarylamine O-acetyltransferase activity Research
Researchers studying N-hydroxyarylamine O-acetyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in arylamine metabolism, carcinogen activation, or arsenical transformation. EDITGENE provides a comprehensive suite of CRISPR-based services to create precisely engineered cell models for functional studies of GO:0046990.
Contact EDITGENE today to design your custom CRISPR model for N-hydroxyarylamine O-acetyltransferase activity research.
Frequently Asked Questions About N-hydroxyarylamine O-acetyltransferase activity
What is N-hydroxyarylamine O-acetyltransferase activity?
It is a molecular function (GO:0046990) that catalyzes the reaction: acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine, as defined by QuickGO.
What genes are involved in N-hydroxyarylamine O-acetyltransferase activity?
Key genes include nhoA in Salmonella typhimurium and Escherichia coli, and NAT1 and NAT2 in mammals, which encode arylamine N-acetyltransferases with O-acetyltransferase activity [1,2,6].
What is the reaction catalyzed by GO:0046990?
The enzyme transfers an acetyl group from acetyl-CoA to an N-hydroxyarylamine, producing an N-acetoxyarylamine and coenzyme A.
Why is N-hydroxyarylamine O-acetyltransferase important in cancer?
It activates arylamine carcinogens by converting N-hydroxyarylamines into reactive N-acetoxyarylamines that can form DNA adducts and cause mutations [1,2].
Which cysteine residue is essential for N-hydroxyarylamine O-acetyltransferase activity?
In Salmonella typhimurium N-hydroxyarylamine O-acetyltransferase, Cys69 is essential for catalysis.
How is N-hydroxyarylamine O-acetyltransferase activity regulated?
In Escherichia coli, reversible acetylation of lysine residues modulates enzymatic activity, and in mammals expression is acetylator genotype-dependent [4,5,7].
What substrates does N-hydroxyarylamine O-acetyltransferase act on?
It acts on N-hydroxyarylamines such as N-hydroxy-2-aminofluorene and arylhydroxamates, and can also acetylate 3-amino-4-hydroxyphenylarsonic acid [2,3].
Is N-hydroxyarylamine O-acetyltransferase the same as arylamine N-acetyltransferase?
They are related activities; in hamster liver, N-hydroxyarylamine O-acetyltransferase co-purifies with polymorphic arylamine N-acetyltransferase, indicating identity [2,5].
How can I study N-hydroxyarylamine O-acetyltransferase activity in the lab?
Common methods include enzyme activity assays with acetyl-CoA and N-hydroxyarylamine substrates, site-directed mutagenesis, and CRISPR knockout or knock-in models [1,4,8].
What CRISPR models are available for GO:0046990 research?
EDITGENE provides knockout, point mutation, knock-in, and overexpression cell models for nhoA, NAT1, NAT2, and related genes to study N-hydroxyarylamine O-acetyltransferase activity.
Conclusion
N-hydroxyarylamine O-acetyltransferase activity (GO:0046990) is a well-defined molecular function that plays a central role in the metabolic activation of arylamine carcinogens and in the biotransformation of aromatic compounds. Its identity with polymorphic arylamine N-acetyltransferase in mammals links it to interindividual differences in cancer susceptibility, while its presence in bacteria underscores its importance in environmental toxicology and biotechnology [1,2,5,7]. Continued research using biochemical assays, mutagenesis, and CRISPR-based models will further clarify its substrate range, regulation, and potential as a target for modulating carcinogen activation and bioremediation [3,4,8].
References
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- 2. Saito K et al.. 1986. N-hydroxyarylamine O-acetyltransferase in hamster liver: identity with arylhydroxamic acid N,O-acetyltransferase and arylamine N-acetyltransferase.. J Biochem 99(6):1689-97 PMID: 3745141
- 3. Huang K et al.. 2020. 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(2) PMID: 31676473
- 4. Zhang QF et al.. 2013. Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.. FEBS J 280(9):1966-79 PMID: 23452042
- 5. Trinidad A et al.. 1990. Purification of hepatic polymorphic arylamine N-acetyltransferase from homozygous rapid acetylator inbred hamster: identity with polymorphic N-hydroxyarylamine-O-acetyltransferase.. Cancer Res 50(24):7942-9 PMID: 2253236
- 6. Yamamura E et al.. 2000. Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli.. Biochim Biophys Acta 1475(1):10-6 PMID: 10806332
- 7. Ogolla F et al.. 1990. Acetylator genotype-dependent expression of arylamine N-acetyltransferase and N-hydroxyarylamine O-acetyltransferase in Syrian inbred hamster intestine and colon. Identity with the hepatic acetylation polymorphism.. Drug Metab Dispos 18(5):680-5 PMID: 1981720
- 8. Watanabe M et al.. 1992. 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(12):8429-36 PMID: 1569093
