Structure of RdxA - an oxygen-insensitive nitroreductase essential for metronidazole activation inHelicobacter pylori
Author:
Affiliation:
1. Structural Biology Unit; CIC bioGUNE, Bizkaia Technology Park; Derio; Spain
2. Division of Infectious Diseases and International Health; Department of Medicine; University of Virginia Health System; Charlottesville; VA; USA
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.12020/fullpdf
Reference40 articles.
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2. Kinetic and structural characterisation of Escherichia coli nitroreductase mutants showing improved efficacy for the prodrug substrate CB1954;Race;J Mol Biol,2007
3. Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases;Koder;Biochemistry,2002
4. Two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H nitroreductase: description of quantitative structure-activity relationships;Nivinskas;Acta Biochim Pol,2000
5. Metronidazole resistance in Helicobacter pylori is due to null mutations in a gene (rdxA) that encodes an oxygen-insensitive NADPH nitroreductase;Goodwin;Mol Microbiol,1998
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