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

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

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) a...

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Veröffentlicht in:The Journal of infectious diseases 1997-09, Vol.176 (3), p.722-727
Hauptverfasser: 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: Artikel
Sprache:eng
Schlagworte:
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
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Zusammenfassung: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
ISSN:0022-1899
1537-6613
DOI:10.1086/514096