TY - JOUR
T1 - Molecular and Biochemical Characterization of a Distinct Type of Fructose-1,6- Bisphosphatase from Pyrococcus furiosus
AU - Verhees, C.H.
AU - Akkerboom, J.
AU - Schiltz, J.
AU - de Vos, W.M.
AU - van der Oost, J.
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
U2 - 10.1128/JB.184.12.3401-3405.2002
DO - 10.1128/JB.184.12.3401-3405.2002
M3 - Article
SN - 0021-9193
VL - 184
SP - 3401
EP - 3405
JO - Journal of Bacteriology
JF - Journal of Bacteriology
ER -