Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Synonyms
fructose-1,6-bisphosphatase, fructose 1,6-bisphosphatase, fructose bisphosphatase, fructose-bisphosphatase, fructose 1,6-diphosphatase, fbp-1, fructose diphosphatase, fru-1,6-p2ase, cytosolic fbpase, cfbp1,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 1,6-bisphosphatase
-
D-fructose 1,6-diphosphatase
-
-
-
-
D-fructose-1,6-bisphosphatase
-
-
-
-
D-fructose-1,6-bisphosphate 1-phosphohydrolase
-
-
-
-
D-fructose-1,6-bisphosphate phosphatase
-
-
-
-
fructose 1,6-bisphosphatase
fructose 1,6-bisphosphate 1-phosphatase
-
-
-
-
fructose 1,6-bisphosphate phosphatase
-
-
-
-
fructose 1,6-diphosphatase
-
-
-
-
fructose 1,6-diphosphate phosphatase
-
-
-
-
fructose bisphosphate phosphatase
-
-
-
-
fructose diphosphatase
-
-
-
-
fructose diphosphate phosphatase
-
-
-
-
hexose bisphosphatase
-
-
-
-
hexose diphosphatase
-
-
-
-
hexosediphosphatase
-
-
-
-
fructose 1,6-bisphosphatase
-
-
-
-
fructose 1,6-bisphosphatase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
?
D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
?
ribulose 1,5-bisphosphate + H2O
ribulose 5-phosphate + phosphate
15% of activity obtained with D-fructose 1,6-bisphosphate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 2,6-bisphosphate
AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
D-glucose 6-phosphate
allosteric inhibition. FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to glucose 6-phosphate. Glc-6-P and AMP are synergistic inhibitors
D-fructose 1,6-bisphosphate
substrate inhibition at high concentrations
D-fructose 2,6-bisphosphate
-
-
fructose 1,6-diphosphate
-
substrate inhibition above 0.05 M
KCl
50 mM, residual activity 20%
pseudo-tetrapeptide OC252
-
the inhibition is synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+ and, uncompetitive with respect to fructose 1,6-bisphosphate
AMP
-
AMP
AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
AMP
FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to AMP. Glc-6-P and AMP are synergistic inhibitors
AMP
-
-
AMP
-
50% inhibition at 0.015 mM
AMP
-
transformation of enzyme to inactive T-state, inhibition shows quarternary transition and cooperativity
ATP
-
ATP
1 mM, reduces activity by 40%
phosphate
-
additional information
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
-
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
not: AMP
-
additional information
-
not: AMP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0014 - 0.016
D-fructose 1,6-bisphosphate
0.00094 - 0.2
D-fructose 1,6-bisphosphate
1
D-Fructose 1-phosphate
pH 7.7
0.035
D-fructose-1,6-bisphosphate
pH 7.7
0.1
fructose 1,6-bisphosphate
wild-type
0.002
fructose 1,6-diphosphate
-
-
0.0014
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
0.0017
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
0.016
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.00094
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
0.0012
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
0.0154
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
0.06
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
0.07
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8 - 26
D-fructose 1,6-bisphosphate
1.1 - 22
D-fructose 1,6-bisphosphate
2.5
fructose 1,6-bisphosphate
wild-type
additional information
additional information
-
8
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
24
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
26
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
1.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
1.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
5.4
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
5.7
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
7.5
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
11.3
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
14
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
14.6
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
20
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
22
D-fructose 1,6-bisphosphate
-
pH 7.5
additional information
additional information
-
-
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Babul, J.; Guixe, V.
Fructose bisphosphatase from Escherichia coli. Purification and characterization
Arch. Biochem. Biophys.
225
944-949
1983
Escherichia coli
brenda
Kelley-Loughnane, N.; Biolsi, S.A.; Gibson, K.M.; Lu, G.; Hehir, M.J.; Phelan, P.; Kantrowitz, E.R.
Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase
Biochim. Biophys. Acta
1594
6-16
2002
Escherichia coli, Sus scrofa (P00636), Sus scrofa
brenda
Donahue, J.L.; Bownas, J.L.; Niehaus, W.G.; Larson, T.J.
Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli
J. Bacteriol.
182
5624-5627
2000
Escherichia coli (P0A9C9), Escherichia coli
brenda
Choe, J.Y.; Nelson, S.W.; Arienti, K.L.; Axe, F.U.; Collins, T.L.; Jones, T.K.; Kimmich, R.D.; Newman, M.J.; Norvell, K.; Ripka, W.C.; Romano, S.J.; Short, K.M.; Slee, D.H.; Fromm, H.J.; Honzatko, R.B.
Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors
J. Biol. Chem.
278
51176-51183
2003
Escherichia coli
brenda
Jang, H.K.; Lee, S.W.; Lee, Y.H.; Hahn, T.R.
Purification and characterization of a recombinant pea cytoplasmic fructose-1,6-bisphosphatase
Protein Expr. Purif.
28
42-48
2003
Escherichia coli, Spinacia oleracea, Sus scrofa, Pisum sativum (Q8RW99), Pisum sativum
brenda
Iancu, C.V.; Mukund, S.; Fromm, H.J.; Honzatko, R.B.
R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase
J. Biol. Chem.
280
19737-19745
2005
Escherichia coli
brenda
Hines, J.K.; Fromm, H.J.; Honzatko, R.B.
Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase
J. Biol. Chem.
281
18386-18393
2006
Escherichia coli (P0A993), Escherichia coli
brenda
Hines, J.K.; Fromm, H.J.; Honzatko, R.B.
Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state
J. Biol. Chem.
282
11696-11704
2007
Escherichia coli (P0A993), Escherichia coli
brenda
Hines, J.K.; Kruesel, C.E.; Fromm, H.J.; Honzatko, R.B.
Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch
J. Biol. Chem.
282
24697-24706
2007
Escherichia coli (P0A993), Escherichia coli
brenda
Hines, J.K.; Chen, X.; Nix, J.C.; Fromm, H.J.; Honzatko, R.B.
Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition
J. Biol. Chem.
282
36121-36131
2007
Sus scrofa (P00636), Sus scrofa, Escherichia coli (P0A993), Escherichia coli
brenda
Brown, G.; Singer, A.; Lunin, V.V.; Proudfoot, M.; Skarina, T.; Flick, R.; Kochinyan, S.; Sanishvili, R.; Joachimiak, A.; Edwards, A.M.; Savchenko, A.; Yakunin, A.F.
Structural and biochemical characterization of the type II D-fructose-1,6-bisphosphatase GlpX from Escherichia coli
J. Biol. Chem.
284
3784-3792
2009
Escherichia coli (P0A9C9), Escherichia coli (P21437), Escherichia coli
brenda
Xu, J.Z.; Zhang, J.L.; Guo, Y.F.; Jia, Q.D.; Zhang, W.G.
Heterologous expression of Escherichia coli fructose-1,6-bisphosphatase in Corynebacterium glutamicum and evaluating the effect on cell growth and L-lysine production
Prep. Biochem. Biotechnol.
44
493-509
2014
Escherichia coli
brenda