Mode of Binding of Pyrroloquinoline Quinone to Glucose Dehydrogenase from Acinetobacter Calcoaceticus

  • Helmut Görisch
  • Otto Geiger
  • Martin Adler

Abstract

In a number of Gram-negative bacteria a quinoprotein glucose deydrogenase is found, which will loose its prosthetic group, when dialysed against buffer containing EDTA. The apoform of the enzyme can be converted to active holoenzyme by pyrroloquinoline quinone (PQQ) in the presence of Mg2+ or Ca2+ ions. In contrast the quinoprotein glucose dehydrogenase from Gluconobacter suboxidans (Ameyama et al., 1981) and from Acinetobacter calcoaceticus (Dokter et al., 1986; Geiger and Görisch, 1986) are not inactivated by dialysis against EDTA-containing buffers. However glucose dehydrogenase from A. calcoaceticus is reversibly inactivated by heat treatment, and restoration of active enzyme depends on the presence of PQQ and Ca2+ ions.

Keywords

Sodium Acetate Buffer Biological Chemistry Anion Exchange Resin Prosthetic Group Heat Inactivation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Ameyama M, Shinagawa E, Matsushita K and Adachi O, 1981. D-Glucose Dehydrogenase of Gluconobacter suboxidans: Solubilization, Purification and Characterization. Agricultural and Biological Chemistry 45: 851–861CrossRefGoogle Scholar
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  4. Geiger O and Görisch H, 1986. Crystalline Quinoprotein Glucose Dehydrogenase from Acinetobacter calcoaceticus. Biochemistry 25: 6043–6048CrossRefGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1989

Authors and Affiliations

  • Helmut Görisch
    • 1
  • Otto Geiger
    • 1
  • Martin Adler
    • 1
  1. 1.Institut für MikrobiologieUniversität HohenheimStuttgart 70Germany

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