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Journal of Bacteriology, June 2001, p. 3417-3427, Vol. 183, No. 11
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.11.3417-3427.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

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

Claudine Deloménie,1 Sylvaine Fouix,1 Sandrine Longuemaux,1 Naïma Brahimi,2 Chantal Bizet,3 Bertrand Picard,4 Erick Denamur,1 and Jean-Marie Dupret1,*

INSERM U4581 and Laboratoire d'Étude de Génétique Bactérienne dans les Infections de l'Enfant EA3105,2 Hôpital Robert Debré, 75019 Paris, Collection de l'Institut Pasteur, 75724 Paris Cedex 15,3 and Laboratoire de Microbiologie et de Santé Publique, Centre Hospitalier Universitaire, 29609 Brest Cedex,4 France

Received 3 October 2000/Accepted 19 March 2001

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.

* Corresponding author. Present address: CNRS UMR 7000, Faculté de Médecine Pitié-Salpêtrière, 105 boulevard de l'Hôpital, 75013 Paris, France. Phone: (33 1) 53 60 08 03. Fax: (33 1) 53 60 08 02. E-mail: jmdupret{at}infobiogen.fr.

Journal of Bacteriology, June 2001, p. 3417-3427, Vol. 183, No. 11
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.11.3417-3427.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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