Within the SulfoSYS (Sulfolobus Systems Biology) project, the effect of temperature on a metabolic network is investigated at the systems level. Sulfolobus solfataricus utilizes an unusual branched ED (Entner–Doudoroff) pathway for sugar degradation that is promiscuous for glucose and galactose. In the course of metabolic pathway reconstruction, a glucose dehydrogenase isoenzyme (GDH-2, SSO3204) was identified. GDH-2 exhibits high similarity to the previously characterized GDH-1 (SSO3003, 61% amino acid identity), but possesses different enzymatic properties, particularly regarding substrate specificity and catalytic efficiency. In contrast with GDH-1, which exhibits broad substrate specificity for C5 and C6 sugars, GDH-2 is absolutely specific for glucose. The comparison of kinetic parameters suggests that GDH-2 might represent the major player in glucose catabolism via the branched ED pathway, whereas GDH-1 might have a dominant role in galactose degradation via the same pathway as well as in different sugar-degradation pathways.
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February 2011
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Conference Article|
January 19 2011
An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?
Patrick Haferkamp;
Patrick Haferkamp
*Faculty of Chemistry, Biofilm Centre, Molecular Enzyme Technology and Biochemistry, University of Duisburg-Essen, Universitätsstrasse, Building S03 V03 F44, 45117 Essen, Germany
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Simone Kutschki;
Simone Kutschki
*Faculty of Chemistry, Biofilm Centre, Molecular Enzyme Technology and Biochemistry, University of Duisburg-Essen, Universitätsstrasse, Building S03 V03 F44, 45117 Essen, Germany
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Jenny Treichel;
Jenny Treichel
*Faculty of Chemistry, Biofilm Centre, Molecular Enzyme Technology and Biochemistry, University of Duisburg-Essen, Universitätsstrasse, Building S03 V03 F44, 45117 Essen, Germany
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Hatim Hemeda;
Hatim Hemeda
†Department of Otorhinolaryngology, University Hospital of Essen, Hufelandstrasse 55, 45147 Essen, Germany
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Karsten Sewczyk;
Karsten Sewczyk
‡Faculty of Biology and Geography, Center for Medical Biotechnology, Bioinformatics, University of Duisburg-Essen, Universitätsstrasse, Building S03 S03 A26, 45117 Essen, Germany
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Daniel Hoffmann;
Daniel Hoffmann
‡Faculty of Biology and Geography, Center for Medical Biotechnology, Bioinformatics, University of Duisburg-Essen, Universitätsstrasse, Building S03 S03 A26, 45117 Essen, Germany
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Melanie Zaparty;
Melanie Zaparty
1
*Faculty of Chemistry, Biofilm Centre, Molecular Enzyme Technology and Biochemistry, University of Duisburg-Essen, Universitätsstrasse, Building S03 V03 F44, 45117 Essen, Germany
1To whom correspondence should be addressed (email bettina.siebers@uni-due.de).
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Bettina Siebers
Bettina Siebers
1
*Faculty of Chemistry, Biofilm Centre, Molecular Enzyme Technology and Biochemistry, University of Duisburg-Essen, Universitätsstrasse, Building S03 V03 F44, 45117 Essen, Germany
1To whom correspondence should be addressed (email bettina.siebers@uni-due.de).
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Publisher: Portland Press Ltd
Received:
August 15 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (1): 77–81.
Article history
Received:
August 15 2010
Citation
Patrick Haferkamp, Simone Kutschki, Jenny Treichel, Hatim Hemeda, Karsten Sewczyk, Daniel Hoffmann, Melanie Zaparty, Bettina Siebers; An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?. Biochem Soc Trans 1 February 2011; 39 (1): 77–81. doi: https://doi.org/10.1042/BST0390077
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