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Gene Review:

nfsA - nitroreductase A

Escherichia coli UTI89

Carroll, C.C. et al., Paterson, E.S. et al., Whiteway, J. et al., Lightfoot, R.T. et al., Yin, H. et al.

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Disease relevance of nfsA

We tested the hypothesis that these nitroreductases are capable of reducing 3-nitrotyrosine in proteins and peptides, as well as in free amino acids using wild-type and nfsA nfsB mutant strains of Escherichia coli [1].

High impact information on nfsA

These results indicate that the nfsA and nfsB enzymes do not reduce 3-nitrotyrosine [1].
The transcription start site (TSS) of nfsA was located upstream of the ybjC gene, a small open reading frame of unknown function located directly upstream of nfsA, suggesting that these two genes form an operon [2].
One member of the soxRS regulon, nfsA, encodes the major oxygen-insensitive nitroreductase in Escherichia coli which catalyzes the reduction of nitroaromatic and nitroheterocyclic compounds by NADPH [2].
Our studies demonstrate that first-step resistance to furazolidone or nitrofurazone results from an nfsA mutation, while the increased resistance associated with second-step mutants is a consequence of an nfsB mutation [3].
We have characterized the nfsA and nfsB genes of a large number of nitrofuran-resistant mutants of Escherichia coli and have correlated mutation with cell extract nitroreductase activity [3].

Chemical compound and disease context of nfsA

Whether the oxygen-insensitive E. coli nitroreductases, encoded by nfsA and nfsB, directly catalyze the TNT reduction or account for the complete TNT transformation pathway, remains to be determined [4].

Biological context of nfsA

Our studies show that the nfsA gene encodes a product that is extremely effective in the metabolic activation of a range of structurally diverse nitrosubstituted compounds [5].
We have designed and constructed a series of plasmids that contain the major and/or minor Escherichia coli nitroreductase genes, nfsA and nfsB, in different combinations with R plasmid mucA/B genes and the Salmonella typhimurium OAT gene [5].

Associations of nfsA with chemical compounds

Stimulation of nfsA nfsB activity with paraquat had no effect on 3-nitrotyrosine reduction [1].

References

Oxygen-insensitive nitroreductases of Escherichia coli do not reduce 3-nitrotyrosine. Lightfoot, R.T., Shuman, D., Ischiropoulos, H. Free Radic. Biol. Med. (2000) [Pubmed]
Regulation of the nfsA Gene in Escherichia coli by SoxS. Paterson, E.S., Boucher, S.E., Lambert, I.B. J. Bacteriol. (2002) [Pubmed]
Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. Whiteway, J., Koziarz, P., Veall, J., Sandhu, N., Kumar, P., Hoecher, B., Lambert, I.B. J. Bacteriol. (1998) [Pubmed]
Reductive transformation of TNT by Escherichia coli: pathway description. Yin, H., Wood, T.K., Smets, B.F. Appl. Microbiol. Biotechnol. (2005) [Pubmed]
Salmonella typhimurium mutagenicity tester strains that overexpress oxygen-insensitive nitroreductases nfsA and nfsB. Carroll, C.C., Warnakulasuriyarachchi, D., Nokhbeh, M.R., Lambert, I.B. Mutat. Res. (2002) [Pubmed]

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