Role of metal ions on the activity of Mycobacterium tuberculosis pyrazinamidase (Articolo in rivista)

Type
Label
  • Role of metal ions on the activity of Mycobacterium tuberculosis pyrazinamidase (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Alternative label
  • Sheen, P., Ferrer, P., Gilman, R.H., Christiansen, G., Moreno-Román, P., Gutiérrez, A.H., Sotelo, J., Evangelista, W., Fuentes, P., Rueda, D., Flores, M., Olivera, P., Solis, J., Pesaresi, A., Lamba, D., Zimic, M. (2012)
    Role of metal ions on the activity of Mycobacterium tuberculosis pyrazinamidase
    in The American journal of tropical medicine and hygiene (Online)
    (literal)
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  • Sheen, P., Ferrer, P., Gilman, R.H., Christiansen, G., Moreno-Román, P., Gutiérrez, A.H., Sotelo, J., Evangelista, W., Fuentes, P., Rueda, D., Flores, M., Olivera, P., Solis, J., Pesaresi, A., Lamba, D., Zimic, M. (literal)
Pagina inizio
  • 153 (literal)
Pagina fine
  • 161 (literal)
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  • 87 (literal)
Rivista
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  • 9 (literal)
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  • 1 (literal)
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  • PubMe (literal)
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
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  • Sheen, P. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Ferrer, P. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Gilman, R.H. - Department of International Health, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, United States; Christiansen, G. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Moreno-Román, P. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Gutiérrez, A.H. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Sotelo, J. - - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Evangelista, W. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Fuentes, P. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Rueda, D. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Flores, M. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru; Olivera, P. - Instituto Peruano de Energia Nuclear, Lima, Peru; Solis, J. - Instituto Peruano de Energia Nuclear, Lima, Peru Pesaresi, A. - Istituto di Cristallografia, Consiglio Nazionale Delle Ricerche, Area Science Park-Basovizza, Trieste, Italy Lamba, D. - Istituto di Cristallografia, Consiglio Nazionale Delle Ricerche, Area Science Park-Basovizza, Trieste, Italy Zimic, M. - Laboratorios de Investigación Y Desarrollo, Facultad de Ciencias, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, San Martín de Porres, Lima 31, Peru (literal)
Titolo
  • Role of metal ions on the activity of Mycobacterium tuberculosis pyrazinamidase (literal)
Abstract
  • Pyrazinamidase of Mycobacterium tuberculosis catalyzes the conversion of pyrazinamide to the active molecule pyrazinoic acid. Reduction of pyrazinamidase activity results in a level of pyrazinamide resistance. Previous studies have suggested that pyrazinamidase has a metal-binding site and that a divalent metal cofactor is required for activity. To determine the effect of divalent metals on the pyrazinamidase, the recombinant wild-type pyrazinamidase corresponding to the H37Rv pyrazinamide-susceptible reference strain was expressed in Escherichia coli with and without a carboxy terminal. His-tagged pyrazinamidase was inactivated by metal depletion and reactivated by titration with divalent metals. Although Co(2+), Mn(2+), and Zn(2+) restored pyrazinamidase activity, only Co(2+) enhanced the enzymatic activity to levels higher than the wild-type pyrazinamidase. Cu(2+), Fe(2+), Fe(3+), and Mg(2+) did not restore the activity under the conditions tested. Various recombinant mutated pyrazinamidases with appropriate folding but different enzymatic activities showed a differential pattern of recovered activity. X-ray fluorescence and atomic absorbance spectroscopy showed that recombinant wild-type pyrazinamidase expressed in E. coli most likely contained Zn. In conclusion, this study suggests that M. tuberculosis pyrazinamidase is a metalloenzyme that is able to coordinate several ions, but in vivo, it is more likely to coordinate Zn(2+). However, in vitro, the metal-depleted enzyme could be reactivated by several divalent metals with higher efficiency than Zn. (literal)
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