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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Escherichia coli and UniProt Accession P0A9C9
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3.1.3.11 fructose-bisphosphataseIUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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Word Map
- 3.1.3.11
- fbpases
-
gluconeogenesis
-
gluconeogenic
- amp
- chloroplast
- phosphoenolpyruvate
-
carboxykinase
- glycogen
- glucose-6-phosphatase
-
phosphofructokinase
- hexokinase
- 2,6-bisphosphate
- spinach
- malate
- thioredoxins
- carboxylase
- starch
- co2
- glucokinase
- phosphorylase
-
6-phosphatase
- fructose-2,6-bisphosphate
- pepck
- trx
- fructose-6-phosphate
- 3-phosphoglycerate
-
nadp-malate
- oleracea
- dihydroxyacetone
- g6pase
- ribulose
- ribulose-1,5-bisphosphate
- triose
-
calvin
- glucagon
- rubisco
-
sucrose-phosphate
-
light-activated
-
amp-dependent
-
antihyperglycemic
- phosphoribulokinase
- 6-phosphofructo-1-kinase
-
calvin-benson
-
monophosphatase
- rubp
- ribulose-5-phosphate
- biofuel production
- synthesis
- medicine
- biotechnology
- molecular biology
- drug development
- diagnostics
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4.1.1.39
-
t-states
-
2.7.1.11
-
triose-phosphate
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CY-F1
-
-
-
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D-fructose 1,6-diphosphatase
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-
-
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D-fructose-1,6-bisphosphatase
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-
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D-fructose-1,6-bisphosphate 1-phosphohydrolase
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-
-
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D-fructose-1,6-bisphosphate phosphatase
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-
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FBPase
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-
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Fru-1,6-P2ase
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-
-
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fructose 1,6-bisphosphatase
fructose 1,6-bisphosphate 1-phosphatase
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-
-
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fructose 1,6-bisphosphate phosphatase
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-
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fructose 1,6-diphosphatase
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-
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fructose 1,6-diphosphate phosphatase
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-
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fructose bisphosphate phosphatase
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-
-
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fructose diphosphatase
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-
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fructose diphosphate phosphatase
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-
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hexose bisphosphatase
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-
-
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hexose diphosphatase
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-
-
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hexosediphosphatase
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-
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RAE-30
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-
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fructose 1,6-bisphosphatase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate 1-phosphohydrolase
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
CAS REGISTRY NUMBER
COMMENTARY
9001-52-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-diphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
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
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?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mg2+
Mn2+
Mn2+
the omission of 2 mM Mn2+ in assay results in 90% loss of activity
Mn2+
divalent metal cations are required for enzymatic activity. Mn2+ supports activity of GlpX and YggF
Mn2+
divalent metal cations are required for enzymatic activity. However, only Mn2+ supports activity of GlpX and YggF
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6-bisphosphate
substrate inhibition at high concentrations
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
pseudo-tetrapeptide OC252
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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
-
transformation of enzyme to inactive T-state, inhibition shows quarternary transition and cooperativity
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
D-fructose 2,6-bisphosphate
AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
mechanism of activation involves binding of anionic ligands which bind to allosteric activation sites, which in turn stabilize a tetramer and a polypeptide fold that obstructs AMP binding
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additional information
-
mechanism of activation involves binding of anionic ligands which bind to allosteric activation sites, which in turn stabilize a tetramer and a polypeptide fold that obstructs AMP binding
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0022
AMP
Escherichia coli
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0181
AMP
Escherichia coli
22°C, pH 7.5, assay is initiated by the addition of enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
-
activity ratio at pH 7.5 to pH 9.5 is 3.5 for wild-type, 3.9 for mutant L54A
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli has two class II D-fructose 1,6-bisphosphatase GlpX and YggF
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
heterologous expression in Corynebacterium glutamicum leads to a recombinant protein that is insensitive to fructose 1-phosphate and fructose 2,6-bisphosphate, whereas the homologous fructose-1,6-bisphosphatase is inhibited by fructose 1-phosphate and fructose 2,6-bisphosphate. The relative enzyme activity of heterologous fructose-1,6-bisphosphatase is 90.8% and 89.1% during supplement with 3 mM fructose 1-phosphate and fructose 2,6-bisphosphate, respectively. Phosphoenolpyruvate is an activator of heterologous fructose-1,6-bisphosphatase, whereas the homologous fructose-1,6-bisphosphatase is very sensitive to phosphoenolpyruvate. Overexpression of the heterologous fructose 1,6-bisphosphatase in wild-type Corynebacterium glutamicum has no effect on L-lysine production, but fructose-1,6-bisphosphatase activities are increased 9- to 13fold. Overexpression increases L-lysine production in Corynebacterim glutamicum lysC(T311I) by 57.3% on fructose, 48.7% on sucrose, and 43% on glucose. The dry cell weight and maximal specific growth rate are increased by overexpression of heterologous fructose 1,6-bisphosphatase
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
crystallization data, enzyme is in a quarternary state between canonical R- and T-state of Sus scrofa enzyme
tetramer
at physiologically relevant concentrations, phosphoenolpyruvate and citrate stabilize an active tetramer over a less active enzyme form of mass comparable with that of a dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of GlpX is determined in a free state and in the complex with a D-fructose 1,6-bisphosphate or inhibitor (phosphate). The crystal structure of the ligand-free GlpX reveals a compact, globular shape with two alpha/beta-sandwich domains. The core fold of GlpX is structurally similar to that of Li+-sensitive phosphatases implying that they have a common evolutionary origin and catalytic mechanism. The structure of the GlpX complex with D-fructose 1,6-bisphosphate reveals that the active site is located between two domains and accommodates several conserved residues coordinating two metal ions and the substrate. The third metal ion is bound to phosphate 6 of the substrate. Phosphate (inhibitor) binds to the active site
crystals of AMP/glucose 6-phosphate/enzyme complexes are grown by hanging drop in vapor diffusion
crystals of native and selenomethionine-substituted proteins are grown by hanging drop in vapor diffusion method, citrate-bound crystals and phosphoenolpyruvate-bound crystals
hanging drops in vapor diffusion, crystals of FBPase with citrate and fructose 2,6-bisphosphate
mutant L54A, in presence of AMP. Growth of crystals in a T-and a R-like conformation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D186A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.2 (wild-type: 5.7/sec)
E59A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.1 (wild-type: 5.7/sec)
K239A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 7.5 (wild-type: 5.7/sec)
K29A
Km (mM) (D-fructose 1,6-bisphosphate): 0.06 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 14 (wild-type: 5.7/sec)
R235A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 5.4 (wild-type: 5.7/sec)
L54A
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enzymic activity similar to wild-type, but much less sensitive to inhibition by AMP. Crystallization data in presence of AMP
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babul, J.; Guixe, V.
Fructose bisphosphatase from Escherichia coli. Purification and characterization
Arch. Biochem. Biophys.
225
944-949
1983
Escherichia coli
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
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
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
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
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
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
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
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
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
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
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