Subunit Analyses of a Novel Thermostable Glucose Dehydrogenase Showing Different Temperature Properties According to Its Quaternary Structure

Part of the Applied Biochemistry and Biotechnology book series (ABAB)

Abstract

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 electron transfer subunit quaternary structures 

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

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

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