Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa

Crescente, Vincenzo, Holland, Sinead M., Kashyap, Sapna, Polycarpou, Elena, Sim, Edith and Ryan, Ali (2016) Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa. Biochemical Journal, 473(5), pp. 549-558. ISSN (print) 0264-6021

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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 activity which leads to a proposed role in plant pathogenesis. Azoreductases have also been suggested to play role in the mammalian pathogenesis of Pseudomonas aeruginosa. In view of the importance of P. aeruginosa as a pathogen, we therefore characterised 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 NAD(P)H quinone oxidoreductase activities. In contrast, WrbA is the first enzyme to show NAD(P)H quinone oxidoreductase 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 .

Item Type: Article
Research Area: Biological sciences
Faculty, School or Research Centre: Faculty of Science, Engineering and Computing (until 2017) > School of Life Sciences
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Depositing User: Katrina Clifford
Date Deposited: 29 Mar 2016 10:05
Last Modified: 01 Feb 2017 03:31

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