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KatG is an enzyme that functions as both catalase and 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]
Reference
edit- ^ 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 – via Elsevier.
- ^ 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.
- ^ 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.
- ^ 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 – via Pubmed.