4.5 Article

KatG from Salmonella Typhimurium is a peroxynitritase

Journal

FEBS LETTERS
Volume 584, Issue 8, Pages 1628-1632

Publisher

WILEY
DOI: 10.1016/j.febslet.2010.03.029

Keywords

Peroxynitrite; Dihydrorhodamine; Catalase; Peroxidase; Peroxynitritase

Funding

  1. Biotechnology and Biological Sciences Research Council (UK)
  2. BBSRC [BB/E015883/1] Funding Source: UKRI
  3. Biotechnology and Biological Sciences Research Council [BB/E015883/1] Funding Source: researchfish

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Pathogenic 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 x 10(4) M (1) s (1) at pH 7.4, 25 degrees C. This enzyme was able to reduce dihydrorhodamine oxidation by peroxynitrite to similar 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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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