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Journal of Bacteriology, June 2002, p. 3401-3405, Vol. 184, No. 12
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.12.3401-3405.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6-Bisphosphatase from Pyrococcus furiosus

Corné H. Verhees,1* Jasper Akerboom,1 Emile Schiltz,2 Willem M. de Vos,1 and John van der Oost1

Laboratory of Microbiology, Wageningen University, Wageningen, The Netherlands,1 University of Freiburg, Freiburg, Germany2

Received 12 December 2001/ Accepted 15 March 2002

The Pyrococcus furiosus fbpA gene was cloned and expressed in Escherichia coli, and the fructose-1,6-bisphosphatase produced was subsequently purified and characterized. The dimeric enzyme showed a preference for fructose-1,6-bisphosphate, with a Km of 0.32 mM and a Vmax of 12.2 U/mg. The P. furiosus fructose-1,6-bisphosphatase was strongly inhibited by Li+ (50% inhibitory concentration, 1 mM). Based on the presence of conserved sequence motifs and the substrate specificity of the P. furiosus fructose-1,6-bisphosphatase, we propose that this enzyme belongs to a new family, class IV fructose-1,6-bisphosphatase.

* Corresponding author. Mailing address: Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands. Phone: 31-317-483748. Fax: 31-317-483829. E-mail: corne.verhees{at}algemeen.micr.wau.nl.

Journal of Bacteriology, June 2002, p. 3401-3405, Vol. 184, No. 12
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.12.3401-3405.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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