Characterization of a catalase-peroxidase variant (L333V-KatG) identified in an INH-resistant Mycobacterium tuberculosis clinical isolate
Author:
Funder
Biological and Environmental Research
Argonne National Laboratory
U.S. Department of Energy
Universidad Nacional Autónoma de México
Publisher
Elsevier BV
Reference34 articles.
1. Global Tuberculosis Report 2019 Global tuberculosis Report;WHO,2020
2. Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activities;Cade;Protein Sci.,2010
3. Catalase in peroxidase clothing: interdependent cooperation of two cofactors in the catalytic versatility of KatG;Njuma;Arch. Biochem. Biophys.,2014
4. Isonicotinic acid hydrazide conversion to Isonicotinyl-NAD by catalase-peroxidases;Wiseman;J. Biol. Chem.,2010
5. Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant;Zhao;Biochemistry,2006
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