title: Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa.
abstract: Azoreductases are a family of diverse enzymes found in many pathogenic bacteria as well as distant homologues being present in eukarya. In addition to having azoreductase activity, these enzymes are also suggested to have NAD(P)H quinone oxidoreductase (NQO) activity which leads to a proposed role in plant pathogenesis. Azoreductases have also been suggested to play a role in the mammalian pathogenesis of Pseudomonas aeruginosa. In view of the importance of P. aeruginosa as a pathogen, we therefore characterized recombinant enzymes following expression of a group of putative azoreductase genes from P. aeruginosa expressed in Escherichia coli. The enzymes include members of the arsenic-resistance protein H (ArsH), tryptophan repressor-binding protein A (WrbA), modulator of drug activity B (MdaB) and YieF families. The ArsH, MdaB and YieF family members all show azoreductase and NQO activities. In contrast, WrbA is the first enzyme to show NQO activity but does not reduce any of the 11 azo compounds tested under a wide range of conditions. These studies will allow further investigation of the possible role of these enzymes in the pathogenesis of P. aeruginosa.
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K.
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Crescente
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K.
authors.forename: Sinead M
authors.initials: SM
authors.lastname: Holland
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K.
authors.forename: Sapna
authors.initials: S
authors.lastname: Kashyap
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K.
authors.forename: Elena
authors.initials: E
authors.lastname: Polycarpou
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K. Department of Pharmacology, University of Oxford, Oxford, OX1 3QT, U.K.
authors.forename: Edith
authors.initials: E
authors.lastname: Sim
authors.affiliation: Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K. a.ryan@kingston.ac.uk.
authors.forename: Ali
authors.initials: A
authors.lastname: Ryan
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003067:Coenzymes / Q000378:metabolism; D004138:Dinitrocresols / Q000378:metabolism; D008958:Models, Molecular; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D009536:Niacinamide / Q000378:metabolism; D009583:Nitrofurazone / Q000378:metabolism; D009601:Nitroreductases; D010084:Oxidation-Reduction; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D003067:Coenzymes; D004138:Dinitrocresols; D011994:Recombinant Proteins; C024132:4,6-dinitro-o-cresol; D009536:Niacinamide; D009247:NADH, NADPH Oxidoreductases; D016660:NAD(P)H Dehydrogenase (Quinone); D009601:Nitroreductases; C021106:azoreductase; D009583:Nitrofurazone
keywords: Pseudomonas aeruginosa; YieF; arsenic-resistance protein H (ArsH); azoreductase; mammalian infection; modulator of drug activity B