KatG

KatG is an enzyme that functions as both catalase and peroxidase, a catalase-peroxidase. In Mycobacterium tuberculosis, mutations in KatG are commonly associated with resistance to the antibiotic drug isoniazid, which targets the mycolic acids within M. tuberculosis, and more general multi-drug resistance.[1][2] Due to both its catalase and peroxidase activity, this enzyme protects M. tuberculosis against reactive oxygen species. M. tuberculosis' survival within macrophages depends on the KatG enzyme.[3][4]

References

  1. ^ Johnsson, Kai (1997). "Overexpression, Purification, and Characterization of the Catalase-peroxidase KatG from Mycobacterium tuberculosis". Journal of Biological Chemistry. 272 (5): 2834–2840. doi:10.1074/jbc.272.5.2834. PMID 9006925. S2CID 23882303.
  2. ^ Tracevska, T.; Jansone, I.; Broka, L.; Marga, O.; Baumanis, V. (2002-10-01). "Mutations in the rpoB and katG Genes Leading to Drug Resistance in Mycobacterium tuberculosis in Latvia". Journal of Clinical Microbiology. 40 (10): 3789–3792. doi:10.1128/JCM.40.10.3789-3792.2002. ISSN 0095-1137. PMC 130873. PMID 12354882.
  3. ^ Heym, B (July 1993). "Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis". Journal of Bacteriology. 175 (13): 4255–4259. doi:10.1128/jb.175.13.4255-4259.1993. PMC 204858. PMID 8320241.
  4. ^ Cockerill, FR (1995). "Rapid identification of a point mutation of the Mycobacterium tuberculosis catalase-peroxidase (katG) gene associated with isoniazid resistance". The Journal of Infectious Diseases. 171 (1): 240–245. doi:10.1093/infdis/171.1.240. PMID 7798673.
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