Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus
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.
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dig-wur-nl-wurpubs-1236762024-06-25 Verhees, C.H. Akkerboom, J. Schiltz, J. de Vos, W.M. van der Oost, J. Article/Letter to editor Journal of Bacteriology 184 (2002) ISSN: 0021-9193 Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus 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␒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. en application/pdf https://research.wur.nl/en/publications/molecular-and-biochemical-characterization-of-a-distinct-type-of- 10.1128/JB.184.12.3401-3405.2002 https://edepot.wur.nl/147334 Life Science Wageningen University & Research |
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Life Science Life Science Verhees, C.H. Akkerboom, J. Schiltz, J. de Vos, W.M. van der Oost, J. Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
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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. |
| format |
Article/Letter to editor |
| topic_facet |
Life Science |
| author |
Verhees, C.H. Akkerboom, J. Schiltz, J. de Vos, W.M. van der Oost, J. |
| author_facet |
Verhees, C.H. Akkerboom, J. Schiltz, J. de Vos, W.M. van der Oost, J. |
| author_sort |
Verhees, C.H. |
| title |
Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
| title_short |
Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
| title_full |
Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
| title_fullStr |
Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
| title_full_unstemmed |
Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus |
| title_sort |
molecular and biochemical characterization of a distinct type of fructose-1,6- bisphosphatase from pyrococcus furiosus |
| url |
https://research.wur.nl/en/publications/molecular-and-biochemical-characterization-of-a-distinct-type-of- |
| work_keys_str_mv |
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1813209594616348672 |