Applied Biochemistry and Biotechnology

, Volume 77, Issue 1–3, pp 325–335 | Cite as

Subunit analyses of a novel thermostable glucose dehydrogenase showing different temperature properties according to its quaternary structure

  • Tomohiko Yamazaki
  • Wakako Tsugawa
  • Koji SodeEmail author


We previously reported a novel glucose dehydrogenase (GDH) showing two peaks in the optimum temperature for the reaction at around 45°C and at around 75°C. Each peak derived from hetero-oligomeric enzyme, constructed from two distinct peptides with an α-subunit (MWs 67,000) and β-subunit (MWs 43,000), and a single peptide enzyme containing an α-subunit alone. The function of the two subunits in the thermostable co-factor binding GDH was investigated. The results of spectroscopic analyses indicated that the α-subunit contained an unknown co-factor showing specific fluorescence spectra like pyrroloquinoline quinone (PQQ), and the β-subunit was cytochrome c. Moreover, the results of a urea denaturation and reconstitution experiment suggested that the dissociation of the hetero-oligomeric complex to a single peptide was reversible. The kinetic parameter analyses for glucose and the electron mediator also suggested that the β-subunit was responsible for electron transfer from the catalytic center of the α-subunit to the electron mediator.

Index Entries

Glucose dehydrogenase thermal stability catalytic subunit electron transfer subunit quaternary structures 


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Copyright information

© Humana Press Inc. 1999

Authors and Affiliations

  1. 1.Department of Biotechnology, Faculty of TechnologyTokyo University of Agriculture and TechnologyKoganei-shi, TokyoJapan

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