@article {1593,
	title = {Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus.},
	journal = {Journal of Bacteriology},
	volume = {184},
	year = {2002},
	month = {2002 Jun},
	pages = {3401-5},
	abstract = {<p>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.</p>
},
	keywords = {Amino Acid Sequence, Archaeal Proteins, Cloning, DNA, Fructose-Bisphosphatase, Molecular, Molecular Sequence Data, Pyrococcus furiosus, Sequence Analysis, Substrate Specificity, Temperature},
	issn = {0021-9193},
	author = {Verhees, Corn{\'e} H and Akerboom, Jasper and Schiltz, Emile and de Vos, Willem M and van der Oost, John}
}
