Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus.
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ABSTRACT:
SUBMITTER: Verhees CH
PROVIDER: S-EPMC135107 | biostudies-other | 2002 Jun
REPOSITORIES: biostudies-other
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Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus.
Verhees Corné H CH Akerboom Jasper J Schiltz Emile E de Vos Willem M WM van der Oost John J
Journal of bacteriology 20020601 12
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. furio ...[more]
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