Evidence for arylamine N-acetyltransferase activity in the bacterium Helicobacter pylori

Chung, Jing‐Gung; Wang, H.H.; Tsou, Mei Fen; Hsieh, Sue Er; Lo, Hsueh-Hsia; Yen, Yee S.; Chang, Shih Sheng; Wu, Lii Tzu; Lee, J.H.; Hung, Chi F.

doi:10.1016/s0378-4274(97)03870-8

Cited by 32 publications

(36 citation statements)

References 21 publications

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“…H. pylori acetylated 2-AF much less efficiently than in previous studies (10,18) (Table 2). We were also unable to retrieve a putative NAT sequence from the H. pylori genome database even though two unrelated strains have been now completely sequenced (1,60).…”

Section: Discussioncontrasting

confidence: 52%

“…In prokaryotes, NATs were first described in S. enterica serovar Typhimurium (65) and then in several species of facultative and obligate anaerobes of the dog and human intestinal microflora. NAT activity has been reported in Escherichia coli, Bacteroides vulgatus, Clostridium sporogenes, Lactobacillus bifidus, Proteus vulgaris, Pseudomonas fluorescens, Enterococcus faecalis (48), Staphylococcus aureus (9), Helicobacter pylori (18), Klebsiella pneumoniae (32), Aeromonas hydrophila (15), Enterobacter aerogenes (61), Pseudomonas aeruginosa (33), Lactobacillus acidophilus (11), Citrobacter koseri (39), and Shigella sonnei (62). However, NAT genes have been cloned and their expression products characterized only for S. enterica serovar Typhimurium (57,65), Mycobacterium smegmatis, and Mycobacterium tuberculosis (49).…”

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confidence: 99%

“…ND, not determined; -, no detectable activity. b Values determined in previous studies (18,20). The values given for recombinant human NATs were not included in the statistical comparison.…”

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confidence: 99%

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Identification and Functional Characterization of Arylamine N -Acetyltransferases in Eubacteria: Evidence for Highly Selective Acetylation of 5-Aminosalicylic Acid

et al. 2001

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Arylamine N-acetyltransferase activity has been described in various bacterial species. Bacterial N-acetyltransferases, including those from bacteria of the gut flora, may be involved in the metabolism of xenobiotics, thereby exerting physiopathological effects. We characterized these enzymes further by steady-state kinetics, time-dependent inhibition, and DNA hybridization in 40 species, mostly from the human intestinal microflora. We report for the first time N-acetyltransferase activity in 11 species of Proteobacteriaceae from seven genera: Citrobacter amalonaticus, Citrobacter farmeri, Citrobacter freundii, Klebsiella ozaenae, Klebsiella oxytoca, Klebsiella rhinoscleromatis, Morganella morganii, Serratia marcescens, Shigella flexneri, Plesiomonas shigelloides, and Vibrio cholerae. We estimated apparent kinetic parameters and found that 5-aminosalicylic acid, a compound efficient in the treatment of inflammatory bowel diseases, was acetylated with a catalytic efficiency 27 to 645 times higher than that for its isomer, 4-aminosalicylic acid. In contrast, para-aminobenzoic acid, a folate precursor in bacteria, was poorly acetylated. Of the wild-type strains studied, Pseudomonas aeruginosa was the best acetylator in terms of both substrate spectrum and catalytic efficiency. DNA hybridization with a Salmonella enterica serovar Typhimurium-derived probe suggested the presence of this enzyme in eight proteobacterial and four gram-positive species. Molecular aspects together with the kinetic data suggest distinct functional features for this class of microbial enzymes.The acetyl coenzyme A (AcCoA):arylamine N-acetyltransferases (NAT; EC 2.3.1.5.) catalyze the transfer of an acetyl group from AcCoA to the nitrogen or oxygen atom of primary arylamines, hydrazines, and their N-hydroxylated metabolites. They therefore play important roles in both the detoxification and metabolic activation of numerous xenobiotics. In the Salmonella enterica serovar Typhimurium mutation assays developed by Ames and coworkers (2), the carcinogenic aromatic amines are N-hydroxylated and subsequently O-acetylated before they can exert genotoxic properties. The O-acetylation step is mediated by the NAT of S. enterica serovar Typhimurium, which therefore governs the activity of many promutagens through N-hydroxyarylamine O-acetyltransferase activity (26).NAT isoforms (28) have been detected in several vertebrate species, including human (6), rabbit (53), rat (21), mouse (37), hamster (23), and chicken (47). Partial data are also available for amphibian (30), helminth (12, 16), and insect (66) species. In prokaryotes, NATs were first described in S. enterica serovar Typhimurium (65) and then in several species of facultative and obligate anaerobes of the dog and human intestinal microflora. NAT activity has been reported in Escherichia coli,

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Section: Discussioncontrasting

confidence: 52%

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confidence: 99%

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Identification and Functional Characterization of Arylamine N -Acetyltransferases in Eubacteria: Evidence for Highly Selective Acetylation of 5-Aminosalicylic Acid

et al. 2001

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“…H pylori has been shown to be capable of catalysing nitrosation reactions 19 and participating in N-acetyltransferase activities. 20 It is therefore possible that the presence of the bacteria in the vicinity of dysplastic cells contributes to the progression of the precancerous process. As mentioned above, oxygen radicals induced by bacteria may produce DNA damage.…”

Section: Discussionmentioning

confidence: 99%

Sulphomucins favour adhesion of Helicobacter pylori to metaplastic gastric mucosa.

Bravo

Correa

1999

J Clin Pathol

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“…The very high K m values reported for substrates like PABA and 2-aminofluorene indicate that the acetylation reaction is very inefficient and is probably catalysed by a protein unrelated to the NATs. 34 One prokaryotic NAT homolog deserves further attention. The Rif gene cluster in A. mediterranei that encodes the proteins necessary for the synthesis of rifamycin B includes the gene RifF for rifamycin amide synthase.…”

Section: Reaction Mechanism and Substrate Specificitymentioning

confidence: 99%

Pharmacogenetics of the arylamine N-acetyltransferases

et al. 2002

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The arylamine N-acetyltransferases (NATs) are involved in the metabolism of a variety of different compounds that we are exposed to on a daily basis. Many drugs and chemicals found in the environment, such as those in cigarette smoke, car exhaust fumes and in foodstuffs, can be either detoxified by NATs and eliminated from the body or bioactivated to metabolites that have the potential to cause toxicity and/or cancer. NATs have been implicated in some adverse drug reactions and as risk factors for several different types of cancers. As a result, the levels of NATs in the body have important consequences with regard to an individual's susceptibility to certain druginduced toxicities and cancers. This review focuses on recent advances in the molecular genetics of the human NATs.

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Evidence for arylamine N-acetyltransferase activity in the bacterium Helicobacter pylori

Cited by 32 publications

References 21 publications

Identification and Functional Characterization of Arylamine N -Acetyltransferases in Eubacteria: Evidence for Highly Selective Acetylation of 5-Aminosalicylic Acid

Identification and Functional Characterization of Arylamine N -Acetyltransferases in Eubacteria: Evidence for Highly Selective Acetylation of 5-Aminosalicylic Acid

Sulphomucins favour adhesion of Helicobacter pylori to metaplastic gastric mucosa.

Pharmacogenetics of the arylamine N-acetyltransferases

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