KatG is an enzyme that functions as both catalase and peroxidase. Its mutation is the cause for Mycobacterium (specifically M. tuberculosis) resistance with the drug isoniazid, which targets the mycolic acids within the tuberculosis bacteria.[1] 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.[2][3]
References
- ^ 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.
- ^ 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.
This page was last edited on 24 July 2021, at 20:27