Archives of Microbiology

, Volume 174, Issue 1–2, pp 104–110

Characterization of the inorganic pyrophosphatase from the pathogenic bacterium Helicobacter pylori

  • Guadalupe Oliva
  • Irma Romero
  • Guadalupe Ayala
  • Idanelli Barrios-Jacobo
  • Heliodoro Celis
Original Paper

DOI: 10.1007/s002030000182

Cite this article as:
Oliva, G., Romero, I., Ayala, G. et al. Arch Microbiol (2000) 174: 104. doi:10.1007/s002030000182

Abstract.

A cytoplasmic pyrophosphatase [E.C. 3.6.1.1.] was partially purified from Helicobacter pylori. The molecular mass was estimated to be 103 kDa by gel filtration. Results of SDS-PAGE suggested that the enzyme consists of six identical subunits of 19.1 kDa each. The enzyme specifically catalyzed the hydrolysis of pyrophosphate and was very sensitive to NaF, but not to sodium molybdate. The optimal pH for activity was 8.5. Mg2+ was required for maximal activity; Mn2+, Co2+, and Zn2+ poorly supported hydrolytic activity. The pyrophosphatase had an apparent Km for Mg-PPi2– hydrolysis of 90 µM, and a Vmax estimated at 24.0 µmol Pi min–1 mg–1.

Cytoplasmic inorganic pyrophosphatase Helicobacter pylori Fluoride sensitivity 

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Guadalupe Oliva
    • 1
  • Irma Romero
    • 2
  • Guadalupe Ayala
    • 3
  • Idanelli Barrios-Jacobo
    • 3
  • Heliodoro Celis
    • 1
  1. 1.Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Apartado Postal 70-243, 04510, México, D.F., Mexico
  2. 2.Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, 04510, México, D.F., Mexico
  3. 3.Centro de Investigación de Enfermedades Infecciosas, Instituto Nacional de Salud Pública, Avenida Universidad 655,62508 Cuernavaca, Morelos, Mexico

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