Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus.

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Journal of Bacteriology. 2002 Jun;184(12):3401-5

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Verhees CH, Akerboom J, Schiltz E, de Vos WM, van der Oost J

Note: Research in this publication was not performed at Janelia.

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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 K(m) of 0.32 mM and a V(max) 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.

PMID: 12029059 [PubMed - indexed for MEDLINE]

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Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus.

Note: Research in this publication was not performed at Janelia.

Abstract

PMID: 12029059 [PubMed - indexed for MEDLINE]

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