{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T09:03:40Z","timestamp":1791450220944,"version":"4.3.3"},"reference-count":45,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2016,3,1]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1042\/bj20150856","type":"journal-article","created":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T03:39:12Z","timestamp":1448941152000},"page":"549-558","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Identification of novel members of the bacterial azoreductase family in <i>Pseudomonas aeruginosa<\/i>"],"prefix":"10.1042","volume":"473","author":[{"given":"Vincenzo","family":"Crescente","sequence":"first","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sinead\u00a0M.","family":"Holland","sequence":"additional","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sapna","family":"Kashyap","sequence":"additional","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Polycarpou","sequence":"additional","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edith","family":"Sim","sequence":"additional","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."},{"name":"Department of Pharmacology, University of Oxford, Oxford, OX1 3QT, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali","family":"Ryan","sequence":"additional","affiliation":[{"name":"Faculty of Science, Engineering and Computing, Kingston University, Penhryn Road, Kingston-upon-Thames KT1 2EE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2016,2,24]]},"reference":[{"key":"2021112216354332200_B1","doi-asserted-by":"publisher","first-page":"e98551","DOI":"10.1371\/journal.pone.0098551","article-title":"Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases belong to the same FMN-dependent superfamily of enzymes","volume":"9","author":"Ryan","year":"2014","journal-title":"PLoS One"},{"key":"2021112216354332200_B2","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1016\/j.anaerobe.2011.12.006","article-title":"Identification, Isolation and characterization of a novel azoreductase from Clostridium perfringens","volume":"18","author":"Morrison","year":"2012","journal-title":"Anaerobe"},{"key":"2021112216354332200_B3","doi-asserted-by":"publisher","first-page":"34890","DOI":"10.1074\/jbc.M405404200","article-title":"Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities","volume":"279","author":"Liger","year":"2004","journal-title":"J. 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