13 research outputs found

    KatG fromSalmonellaTyphimurium is a peroxynitritase

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    AbstractPathogenic bacteria elicit protective responses to oxidative and nitrosative stresses. Although such responses are generally distinct, it was recently reported in Mycobacterium tuberculosis that catalase–peroxidase (KatG), a classical defence against peroxides, also exhibits peroxynitritase activity. Here, the katG gene from Salmonella Typhimurium was cloned and protein purified and characterised. An increase in the rate of decomposition of peroxynitrite was observed for KatG from the enterobacterium with a second-order rate constant of 4.2×104M−1s−1 at pH 7.4, 25°C. This enzyme was able to reduce dihydrorhodamine oxidation by peroxynitrite to ∌83%. Given the peroxynitritase activity demonstrated here it is likely that KatG may play a wider role in the detoxification of oxidative stresses than previously thought

    KatG fromSalmonellaTyphimurium is a peroxynitritase

    Get PDF
    AbstractPathogenic bacteria elicit protective responses to oxidative and nitrosative stresses. Although such responses are generally distinct, it was recently reported in Mycobacterium tuberculosis that catalase–peroxidase (KatG), a classical defence against peroxides, also exhibits peroxynitritase activity. Here, the katG gene from Salmonella Typhimurium was cloned and protein purified and characterised. An increase in the rate of decomposition of peroxynitrite was observed for KatG from the enterobacterium with a second-order rate constant of 4.2×104M−1s−1 at pH 7.4, 25°C. This enzyme was able to reduce dihydrorhodamine oxidation by peroxynitrite to ∌83%. Given the peroxynitritase activity demonstrated here it is likely that KatG may play a wider role in the detoxification of oxidative stresses than previously thought
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