3n2s
Structure of NfrA1 nitroreductase from B. subtilisStructure of NfrA1 nitroreductase from B. subtilis
Structural highlights
FunctionNFRA1_BACSU Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H(2)O(2) produced during the oxidative process or added exogenously. STRUCTURED SUMMARY: MINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb:P39605) bind (MI:0407) by X-ray crystallography (MI:0114). NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role.,Cortial S, Chaignon P, Iorga BI, Aymerich S, Truan G, Gueguen-Chaignon V, Meyer P, Morera S, Ouazzani J FEBS Lett. 2010 Aug 18. PMID:20727352[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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