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

C.H. Verhees, J. Akkerboom, J. Schiltz, W.M. de Vos, J. van der Oost

Research output: Contribution to journalArticleAcademicpeer-review

30 Citations (Scopus)

Abstract

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␒nhibitory 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.
Original languageEnglish
Pages (from-to)3401-3405
JournalJournal of Bacteriology
Volume184
DOIs
Publication statusPublished - 2002

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