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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P09201
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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
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2.7.1.11
-
triose-phosphate
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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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-
-
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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
Fru-1,6-P2ase
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-
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fructose 1,6-bisphosphatase
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-
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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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-
-
-
additional information
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily
FBPase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
uni-bi mechanism
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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
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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
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
glucose 1,6-diphosphate + H2O
?
-
about 10% of maximal activity
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-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
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about 5% of maximal activity
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-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
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-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the substrate is bound in its linear, open conformation with the cleavable C1-phosphate positioned deep in the active site
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-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
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-
?
additional information
?
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enzyme influences the connection between DNA damage, aging and oxidative stress
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-
?
additional information
?
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purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
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-
?
additional information
?
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purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
-
-
?
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
best substrate
-
-
?
additional information
?
-
-
enzyme influences the connection between DNA damage, aging and oxidative stress
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is independent of metals, Mg2+, Mn2+, Co2+, Ni2+, Li+, and Ca2+ show no effect on activity
additional information
-
the enzyme is independent of metals, Mg2+, Mn2+, Co2+, Ni2+, Li+, and Ca2+ show no effect on activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
rapid inactivation in vivo by addition of glucose is caused by phosphorylation of the enzyme
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AMP
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the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
fructose 2,6-diphosphate
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the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
additional information
additional information
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
-
additional information
additional information
-
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27000
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
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pH 6.0: about 25% of maximal activity, pH 11.0.: 55% of maximal activity
6.5 - 9.5
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pH 6.5: about 40% of maximal activity, pH 9.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
for the vacuolar-dependent degradation pathway, FBPase is imported into intermediate carriers know as Vid vesicles (vacuole import and degradation) vesicles
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fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily. YK23 represents the first family of metal-independent FBPases and a second FBPase family in eukaryotes
metabolism
-
fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events
physiological function
fructose-1,6-bisphosphatase is a key enzyme of gluconeogenesis and photosynthetic CO2 fixation, catalyzes the hydrolysis of fructose 1,6-bisphosphate to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the core domain with the alpha/beta/alpha-fold is covered by two small cap domains, structures of presence of two phosphate molecules as inhibitor or FBP (a substrate) bound to the active site, overview
additional information
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the core domain with the alpha/beta/alpha-fold is covered by two small cap domains, structures of presence of two phosphate molecules as inhibitor or FBP (a substrate) bound to the active site, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
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fructose 1,6-diphosphatase a is the active non-phosphorylated form of the enzyme. Fructose 1,6-diphosphatase b is the less active phosphorylated form of the enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified selenomethionine-substituted YK23 in apo-form, hanging drop vapor diffusion method, 22°C, purified YK23, at 29 mg/ml, is mixed with 1.5 mg/ml of trypsin solution in 1 mM HCl and 2 mM CaCl2 in a ratio of 1:10 for the apoenzyme and or 1:20 for the phosphate-bound enzyme, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution, containing 0.2 M trilithium citrate, pH 8.1, 16% PEG 3350 and 4% 2-methyl-2,4-pentanediol, 2 days, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E99A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H13A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H178A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H244A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H268A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R181A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R69A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S19A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S65A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W131A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
Y24A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
additional information
-
enzyme deletion mutant, reduced sensitivity to alkylating agent methymethane sulfonate and reduced production of reactive oxygen species. Overexpression of enzyme increases sensitivity to methymethane sulfonate, shortens life span and increases induction of RNR2 gene
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YKR043C, DNA and amino acid sequence determination and analysis, recombinant expression of the N-terminally His6-tagged enzyme, comtaining a tobacco etch virus protease cleavage site, in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
SEC28 (subunit of the coat protein complex I) is required for FBPase degradation. When SEC28 and other coatomer genes are mutated, FBPase degradation is defective and FBPase association with Vid vesicles is impaired
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marcus, F.; Rittenhouse, J.; Moberly, L.; Edelstein, I.; Hiller, E.; Rogers, D.T.
Yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase. Properties of phospho and dephospho forms and of two mutants in which serine 11 has been changed by site-directed mutagenesis
J. Biol. Chem.
263
6058-6062
1988
Saccharomyces cerevisiae
Rogers, D.T.; Hiller, E.; Mitsock, L.; Orr, E.
Characterization of the gene for fructose-1,6-bisphosphatase from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein homology, and expression during growth on glucose
J. Biol. Chem.
263
6051-6057
1988
Saccharomyces cerevisiae, Schizosaccharomyces pombe
Noda, T.; Hoffschulte, H.; Holzer, H.
Characterization of fructose 1,6-bisphosphatase from bakers yeast
J. Biol. Chem.
259
7191-7197
1984
Saccharomyces cerevisiae
Funayama, S.; Molano, J.; Gancedo, C.
Purification and properties of a D-fructose 1,6-bisphosphatase from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
197
170-177
1979
Saccharomyces cerevisiae
Mazon, M.J.
Regulation of yeast fructose-1,6-bisphosphatase by phosphorylation-dephosphorylation
Curr. Top. Cell. Regul.
27
159-169
1985
Saccharomyces cerevisiae
Kitanovic, A.; Wolfl, S.
Fructose-1,6-bisphosphatase mediates cellular responses to DNA damage and aging in Saccharomyces cerevisiae
Mutat. Res.
594
135-147
2006
Saccharomyces cerevisiae
Brown, C.R.; Wolfe, A.B.; Cui, D.; Chiang, H.L.
The vacuolar import and degradation pathway merges with the endocytic pathway to deliver fructose-1,6-bisphosphatase to the vacuole for degradation
J. Biol. Chem.
283
26116-26127
2008
Saccharomyces cerevisiae (P09201)
Kuznetsova, E.; Xu, L.; Singer, A.; Brown, G.; Dong, A.; Flick, R.; Cui, H.; Cuff, M.; Joachimiak, A.; Savchenko, A.; Yakunin, A.F.
Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae
J. Biol. Chem.
285
21049-21059
2010
Saccharomyces cerevisiae (P36136), Saccharomyces cerevisiae
Giardina, B.J.; Chiang, H.L.
The key gluconeogenic enzyme fructose-1,6-bisphosphatase is secreted during prolonged glucose starvation and is internalized following glucose re-feeding via the non-classical secretory and internalizing pathways in Saccharomyces cerevisiae
Plant Signal. Behav.
8
e24936
2013
Saccharomyces cerevisiae
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