MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint mart_nez_j_-2012-1 Structure of RdxA--an oxygen-insensitive nitroreductase essential for metronidazole activation in Helicobacter pylori. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Martínez-Júlvez M., Rojas AL., Olekhnovich I., Espinosa Angarica V., Hoffman PS., Sancho J. FEBS J. (1742-464X) 2012 rdxa_helpy Oxygen-insensitive NADPH nitroreductase HP_0954 rdxA protein protein helpy Helicobacter pylori Campylobacter pylori MKFLDQEKRRQLLNERHSCKMFDSHYEFSSTELEEIAEIARLSPSSYNTQPWHFVMVTDKDLKKQIAAHSYFNEEMIKSASALMVVCSLRPSELLPHGHYMQNLYPESYKVRVIPSFAQMLGVRFNHSMQRLESYILEQCYIAVGQICMGVSLMGLDSCIIGGFDPLKVGEVLEERINKPKIACLIALGKRVAEASQKSRKSKVDAITWL Reduction of a variety of nitroaromatic compounds using NADPH as source of reducing equivalents; two electrons are transferred (By similarity). Capable of reducing metronidazole; inactive rdxA renders the bacterium resistant to this compound. The reduction of metronidazole generates hydroxylamine, a potent mutagen and bactericide mint rdxa-1 1321045 rdxa_helpy RdxA 1321046 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false mint f1 t1