Recombinant Mycobacterium tuberculosis KatG(S315T) Is a Competent Catalase-Peroxidase with Reduced Activity toward Isoniazid

• Published in: The Journal of infectious diseases 1997-09, Vol.176 (3), p.722-727
• Main Authors: Wengenack, Nancy L., Uhl, James R., St. Amand, Allison L., Tomlinson, Andy J., Benson, Linda M., Naylor, Stephen, Kline, Bruce C., Cockerill, Frank R., Rusnak, Frank
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacterial Proteins; Bacteriology; Biochemistry; Biological and medical sciences; Catalase - metabolism; Chromatography, High Pressure Liquid; Enzymes; Escherichia coli; Fundamental and applied biological sciences. Psychology; Genetic mutation; Infectious diseases; Isoniazid - metabolism; Major Articles; Mass spectroscopy; Microbiology; Molecular ions; Molecular Sequence Data; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; Mycobacterium tuberculosis - drug effects; Mycobacterium tuberculosis - enzymology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Peroxidases - biosynthesis; Peroxidases - genetics; Peroxidases - isolation & purification; Peroxidases - metabolism; Plasmids; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Tuberculosis
• ISSN: 0022-1899; 1537-6613
• DOI: 10.1086/514096

The presence of KatG(S315T), a mutation frequently detected in clinical isolates of Mycobacterium tuberculosis, has been associated with loss of catalase-peroxidase activity and resistance to isoniazid therapy. Wild-type KatG and KatG(S315T) were expressed in a heterologous host (Escherichia coli) and purified to homogeneity, and enzymatic activity was measured. The catalase activity for KatG(S315T) was reduced 6-fold, and its peroxidase activity was decreased