ArticleBMC microbiology2017
Identification of Enterococcus faecalis enzymes with azoreductases and/or nitroreductase activity.
Article in BMC microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Cloning, purification and possible use of a Bacillus nitroreductase in biotechnological applications.Scientific reports · 2026Article
- Electrical stress and acid orange 7 synergistically clear the blockage of electron flow in the methanogenesis of low-strength wastewater.Environmental science and ecotechnology · 2024Article
- Sequence similarity network analysis of drug- and dye-modifying azoreductase enzymes found in the human gut microbiome.Archives of biochemistry and biophysics · 2024Article
- The Catalysis Mechanism ofInternational journal of molecular sciences · 2024Article
- Genome-wide analysis of acid tolerance genes of Enterococcus faecalis with RNA-seq and Tn-seq.BMC genomics · 2024Article
- 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
- Cell-Free Protein Synthesis for the Screening of Novel Azoreductases and Their Preferred Electron Donor.Chembiochem : a European journal of chemical biology · 2022Article
- Biodegradation and Detoxification of Azo Dyes by Halophilic/Halotolerant Microflora Isolated From the Salt Fields of Tibet Autonomous Region China.Frontiers in microbiology · 2022Article
- Unraveling Mechanisms and Epidemic Characteristics of Nitrofurantoin Resistance in UropathogenicInfection and drug resistance · 2021Article
- Importance evaluation of spectral lines in Laser-induced breakdown spectroscopy for classification of pathogenic bacteria.Biomedical optics express · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNitroreductases, NAD(P)H dependent flavoenzymes, are found in most of bacterial species. Even if Enterococcus faecalis strains seems to present such activity because of their sensitivity to nitrofurans, no enzyme has been described. Nitroreductases were separated of others reductases due to their capacity to reduce nitro compounds. They are further classified based on their preference in cofactor: NADH and/or NADPH. However, recently, azoreductases have been studied for their strong activity on nitro compounds, especially nitro pro-drugs. This result suggests a crossing in azo and nitro reductase activities. For the moment, no nitroreductase was demonstrated to possess azoreductase activity. But due to sequence divergence and activity specificity linked to substrates, activity prediction is not evident and biochemical characterisation remains necessary. Identifying enzymes active on these two classes of compounds: azo and nitro is of interest to consider a common physiological role.
resultsFour putative nitroreductases, EF0404, EF0648, EF0655 and EF1181 from Enterococcus faecalis V583 were overexpressed as his-tagged recombinant proteins in Escherichia coli and purified following a native or a denaturing/renaturing protocol. EF0648, EF0655 and EF1181 showed nitroreductase activity and their cofactor preferences were in agreement with their protein sequence phylogeny. EF0404 showed both nitroreductase and azoreductase activity. Interestingly, the biochemical characteristics (substrate and cofactor specificity) of EF0404 resembled the properties of the known azoreductase AzoA. But its sequence matched within nitroreductase group, the same as EF0648.
conclusionsWe here demonstrate nitroreductase activity of the putative reductases identified in the Enterococcus faecalis V583 genome. We identified the first nitroreductase able to reduce directly an azo compound, while its protein sequence is close to others nitroreductases. Consequently, it highlights the difficulty in classifying these enzymes solely on the basis of protein sequence alignment and hereby the necessity to experimentally demonstrate the activity. The results provide additional data to consider a broader functionality of these reductases.
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