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Related Experiment Videos

Mycobacterium tuberculosis KatG is a peroxynitritase.

N L Wengenack1, M P Jensen, F Rusnak

  • 1Department of Biochemistry and Molecular Biology and Section of Hematology Research, Mayo Clinic and Foundation, Rochester, Minnesota, 55905, USA.

Biochemical and Biophysical Research Communications
|March 19, 1999
PubMed
Summary

Mycobacterium tuberculosis KatG enzyme efficiently breaks down peroxynitrite, a harmful molecule found in macrophages. This newly identified peroxynitritase activity may help the bacteria survive within host cells.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Mycobacterium tuberculosis (Mtb) survives in the oxidative environment of human macrophages.
  • Mtb is known to be susceptible to reactive nitrogen intermediates like peroxynitrite.
  • The hemoprotein KatG is a known enzyme in Mtb with various functions.

Purpose of the Study:

  • To investigate the potential role of Mycobacterium tuberculosis KatG as a peroxynitritase.
  • To quantify the catalytic efficiency of KatG in decomposing peroxynitrite.

Main Methods:

  • Enzymatic assays were performed to measure the reaction rate of KatG with peroxynitrite.
  • Kinetic parameters, specifically the association rate constant (kapp), were determined at physiological conditions (pH 7.4 and 37°C).

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Main Results:

  • Mycobacterium tuberculosis KatG was found to be an efficient peroxynitritase.
  • KatG exhibited a kapp of 1.4 x 10^5 M^-1s^-1 for peroxynitrite decomposition.
  • This activity was observed at pH 7.4 and 37°C.

Conclusions:

  • The hemoprotein KatG possesses significant peroxynitritase activity.
  • This enzymatic function of KatG may contribute to the persistence of Mycobacterium tuberculosis within macrophages.
  • KatG's ability to neutralize peroxynitrite adds to its known enzymatic repertoire.