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J Biol Chem, Vol. 273, Issue 43, 28149-28154, October 23, 1998

The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic Archaeon Pyrococcus furiosus Represents a Novel Site of Glycolytic Regulation

John van der Oost, Gerti Schut, Servé W. M. Kengen, Wilfred R. Hagen, Michael Thomm^**, and Willem M. de Vos

From the  Laboratory of Microbiology, Wageningen Agricultural University, Hesselink van Suchtelenweg 4, NL-6307 CT Wageningen, The Netherlands, the  Laboratory of Biochemistry, Wageningen Agricultural University, Dreijenlaan 3, NL-6307 HA Wageningen, The Netherlands, and the ^** Institut für Allgemeine Microbiologie, Christian-Albrechts Universität zu Kiel, Am Botanische Garten 1-9, D-24118 Kiel, Germany

The fermentative conversion of glucose in anaerobic hyperthermophilic Archaea is a variant of the classical Embden-Meyerhof pathway found in Bacteria and Eukarya. A major difference of the archaeal glycolytic pathway concerns the conversion of glyceraldehyde-3-phosphate. In the hyperthermophilic archaeon Pyrococcus furiosus, this reaction is catalyzed by an unique enzyme, glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR). Here, we report the isolation, characterization, and transcriptional analysis of the GAPOR-encoding gene. GAPOR is related to a family of ferredoxin-dependent tungsten enzymes in (hyper)thermophilic Archaea and, in addition, to a hypothetical protein in Escherichia coli. Electron paramagnetic resonance analysis of the purified P. furiosus GAPOR protein confirms the anticipated involvement of tungsten in catalysis. During glycolysis in P. furiosus, GAPOR gene expression is induced, whereas the activity of glyceraldehyde-3-phosphate dehydrogenase is repressed. It is discussed that this unprecedented unidirectional reaction couple in the pyrococcal glycolysis and gluconeogenesis gives rise to a novel site of glycolytic regulation that might be widespread among Archaea.

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