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Microbial peroxidase refers to a heterogeneous group of enzymes produced by bacteria, fungi, and other microorganisms that catalyze the reduction of peroxides (typically hydrogen peroxide) by various electron donors. These enzymes are structurally diverse, with most being heme-containing proteins but some being non-heme peroxidases or using alternative cofactors. Key families include cytochrome c peroxidases, catalase–peroxidases, and DyP-type peroxidases. Their main biological role is to protect microbes from oxidative damage by detoxifying hydrogen peroxide and other reactive oxygen species, but they also play important roles in microbial virulence (e.g., evading host immune defenses) and may be essential for survival in hostile or aerobic environments. In pathogens such as Mycobacterium tuberculosis, microbial peroxidase is a validated drug target (e.g., catalase–peroxidase is targeted by isoniazid). The term \"microbial peroxidase\" is non-specific and represents multiple enzyme subfamilies rather than a single, well-defined protein, so further specification is recommended where possible.
Enzyme inhibition: Drugs may block the peroxidase active site, preventing detoxification of hydrogen peroxide and increasing susceptibility to oxidative damage. Suicide substrate inactivation: Some drugs (isoniazid) are enzymatically activated by microbial peroxidase, generating toxic species or radicals.
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