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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Bos taurus

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.11 fructose-bisphosphatase
IUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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This record set is specific for:
Bos taurus
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The taxonomic range for the selected organisms is: Bos taurus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CY-F1
-
-
-
-
D-fructose 1,6-diphosphatase
-
-
-
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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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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
-
-
-
-
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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-
-
-
hexose diphosphatase
-
-
-
-
hexosediphosphatase
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-
-
-
RAE-30
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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-
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 hide
9001-52-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-glycerophosphate + H2O
?
show the reaction diagram
-
substrate at pH 9.0, no activity at pH 6.5
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
D-fructose 1,6-diphosphate + H2O
?
show the reaction diagram
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-diphosphate + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activates
additional information
-
divalent metal ion required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Fluoro-2,4-dinitrobenzene
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
2,5-anhydromannitol 1,6-diphosphate
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-
2-deoxyribose-5-phosphate
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-
5,5'-dithiobis(2-nitrobenzoate)
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up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
D-fructose-2,6-bisphosphate
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fructose 1,6-diphosphate
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at high concentrations
fructose 2,6-diphosphate
fructose 6-phosphate
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product inhibitor
Glutaraldehyde
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-
iodoacetate
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-
nagarse
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stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
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NEM
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
p-mercuribenzoate
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up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
papain
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stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
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phosphate
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product inhibitor
phosphite
-
-
Pronase
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
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Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Fluoro-2,4-dinitrobenzene
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
5,5'-dithiobis-(2-nitrobenzoate)
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
8-hydroxyquinoline
-
activates
citrate
-
activates
EGTA
-
activates
His
-
activation
imidazole
-
activates
Mg2+
-
required
nagarse
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
NEM
-
up to 90% inhibition at pH 6.5-7.0, slight increase of activity at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
p-mercuribenzoate
-
up to 90% inhibition at pH 6.5-7.0, slight increase of activity at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
papain
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stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
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Pronase
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.002
fructose 1,6-diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55 - 14.8
D-fructose 1,6-bisphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00009 - 0.00021
D-fructose-2,6-bisphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19
-
lung tissue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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-
7.2
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7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 10
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pH 6.3: about 30% of maximal activity, pH 10.0: about 45% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F16P1_BOVIN
338
0
36728
Swiss-Prot
other Location (Reliability: 2)
F16P2_BOVIN
339
0
36767
Swiss-Prot
other Location (Reliability: 1)
B2KJ42_BOVIN
338
0
36740
TrEMBL
other Location (Reliability: 2)
A0A3Q1MK34_BOVIN
319
0
34576
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
127000
-
equilibrium sedimentation
130000
140000
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analytical ultracentrifugation
143000
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gel filtration
35500
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4 * 35500, SDS-PAGE
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 35500, SDS-PAGE
additional information
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-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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15 min, 50% loss of activity
additional information
-
fructose 1,6-diphosphate, Mg2+ and Mn2+ protect against thermal inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 7.5-8.0, 10 mM Tris, 1.0 mM EDTA, 3.0 mM MgSO4 or 20 mM beta-glycerophosphate, 1.0 mM fructose 1,6-diphosphate, stable for many months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, F.; Fromm, H.J.
Purification and characterization of fructose-1,6-bisphosphatase from bovine brain
Arch. Biochem. Biophys.
260
609-615
1988
Bos taurus
Manually annotated by BRENDA team
Ganson, N.J.; Fromm, H.J.
Mechanism and regulation of bovine liver fructose-1,6-bisphosphatase
Curr. Top. Cell. Regul.
24
197-207
1984
Bos taurus
Manually annotated by BRENDA team
Nimmo, H.G.; Tipton, K.F.
Fructose-bisphosphatase from ox liver
Methods Enzymol.
90
330-334
1982
Bos taurus
Manually annotated by BRENDA team
Geller, A.M.; Byrne, W.L.
Fructose-1,6-diphosphate from bovine liver
Methods Enzymol.
42C
363-368
1975
Bos taurus
Manually annotated by BRENDA team
Nimmo, H.G.; Tipton, K.F.
The purification of fructose 1,6-diphosphatase from ox liver and its activation by ethylenediaminetetra-acetate
Biochem. J.
145
323-334
1975
Bos taurus
Manually annotated by BRENDA team
Byrne, W.L.; Rajagopalan, G.T.; Griffin, L.D.; Ellis, E.H.; Harris, R.M.; Hochachka, P.; Reid, L.; Geller, A.M.
Bovine hepatic fructose 1,6-diphosphatase: purification and properties
Arch. Biochem. Biophys.
146
118-133
1971
Bos taurus
Manually annotated by BRENDA team
Casazza, J.P.; Stone, S.R.; Fromm, H.J.
Kinetic studies of bovine liver fructose-1,6-bisphosphatase
J. Biol. Chem.
254
4661-4665
1979
Bos taurus
Manually annotated by BRENDA team
Benkovic, S.J.; deMaine, M.M.
Mechanism of action of fructose 1,6-bisphosphatase
Adv. Enzymol. Relat. Areas Mol. Biol.
53
45-82
1981
Bos taurus, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Ovis aries, Mus musculus, Rattus norvegicus, Phocidae, Sus scrofa
Manually annotated by BRENDA team
Rakus, D.; Skalecki, K.; Dzugaj, A.
Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase): liver-like isozymes in mammalian lung tissue
Comp. Biochem. Physiol. B
127
123-134
2000
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa domesticus
Manually annotated by BRENDA team