ArticlePloS one2014
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.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Spatiotemporal coordination of virulence, metabolism, and stress responses shapes infection dynamics ofApplied and environmental microbiology · 2026Article
- Article
- A Potent Quinone Reductase Encoded byMolecules (Basel, Switzerland) · 2026Article
- Genomic and mutational analysis of Pseudomonas syringae pv. tagetis EB037 pathogenicity on sunflower.BMC microbiology · 2025Article
- Profiling sorghum-microbe interactions with a specialized photoaffinity probe identifies key sorgoleone binders inApplied and environmental microbiology · 2024Article
- The dynamic crosslinking between gut microbiota and inflammation during aging: reviewing the nutritional and hormetic approaches against dysbiosis and inflammaging.Biogerontology · 2024Review
- Sequence similarity network analysis of drug- and dye-modifying azoreductase enzymes found in the human gut microbiome.Archives of biochemistry and biophysics · 2024Article
- Mining the Metabolic Capacity of Clostridium sporogenes Aided by Machine Learning.Angewandte Chemie (International ed. in English) · 2024Article
- Transcriptome analysis ofFrontiers in plant science · 2024Article
- Human Gut Microbiota and Drug Metabolism.Microbial ecology · 2023Review
- Gut Microbiome-Wide Search for Bacterial Azoreductases Reveals Potentially Uncharacterized Azoreductases Encoded in the Human Gut Microbiome.Drug metabolism and disposition: the biological fate of chemicals · 2023Article
- Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Review
- MdaB and NfrA, Two Novel Reductases Important in the Survival and Persistence of the Major Enteropathogen Campylobacter jejuni.Journal of bacteriology · 2022Article
- Iron-dependent mutualism betweenISME communications · 2022Article
- Gut microbiota mediates the absorption of FLZ, a new drug for Parkinson's disease treatment.Acta pharmaceutica Sinica. B · 2021Article
- Proteomic Analyses ofFrontiers in cellular and infection microbiology · 2021Article
- Delineating the potential targets of thymoquinone in ESKAPE pathogens using a computational approach.In silico pharmacology · 2021Article
- Comparative genome analyses ofMicrobial genomics · 2020Article
- Mechanistic and Crystallographic Studies of Azoreductase AzoA fromACS chemical biology · 2020Article
- Altered proteome of aPeerJ · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Water soluble quinones are a group of cytotoxic anti-bacterial compounds that are secreted by many species of plants, invertebrates, fungi and bacteria. Studies in a number of species have shown the importance of quinones in response to pathogenic bacteria of the genus Pseudomonas. Two electron reduction is an important mechanism of quinone detoxification as it generates the less toxic quinol. In most organisms this reaction is carried out by a group of flavoenzymes known as NAD(P)H quinone oxidoreductases. Azoreductases have previously been separate from this group, however using azoreductases from Pseudomonas aeruginosa we show that they can rapidly reduce quinones. Azoreductases from the same organism are also shown to have distinct substrate specificity profiles allowing them to reduce a wide range of quinones. The azoreductase family is also shown to be more extensive than originally thought, due to the large sequence divergence amongst its members. As both NAD(P)H quinone oxidoreductases and azoreductases have related reaction mechanisms it is proposed that they form an enzyme superfamily. The ubiquitous and diverse nature of azoreductases alongside their broad substrate specificity, indicates they play a wide role in cellular survival under adverse conditions.
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