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Information on EC 2.7.1.105 - 6-phosphofructo-2-kinase
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EC Tree
2.7.1.105 6-phosphofructo-2-kinaseIUBMB Comments
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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Word Map
- 2.7.1.105
- 2,6-bisphosphate
- fructose-2,6-bisphosphate
- pfkfb3
- 6-phosphofructo-1-kinase
-
camp-dependent
- phosphofructokinase-1
- mgatp
- phosphoenzyme
- medicine
- sn-glycerol
-
cyclic-amp-dependent
-
fru-6-p
-
3-3hglucose
- fbpase-2
- pharmacology
- diagnostics
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2, 6-phosphofructo kinase-2/fructose diphosphatase-2 isoenzyme 3, 6-phosphofructo-2-kinase, 6-phosphofructo-2-kinase/2,6-bisphosphatase 3, 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2
6-phosphofructo-2-kinase
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex
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6-phosphofructose 2-kinase
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-
-
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ATP:D-fructose-6-phosphate 2-phosphotransferase
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-
-
-
fructose 6-phosphate 2-kinase
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-
-
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iPFK2
kinase, 6-phosphofructo-2-(phosphorylating)
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-
-
-
Pfk-2
PFK-2/FBPase
PFK-2/FBPase-2
PFK2/FBPase2
PFKFB-3
PFKFB1
PFKFB2
PFKFB3
PFKFB4
phosphofructokinase 2
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-
-
-
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
-
-
-
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
PFK-2/FBPase-2
the bifunctional enzyme has 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
PFK-2/FBPase-2
-
the bifunctional enzyme has 6-phosphofructo-2-kinase and fructose 2,6-bisphosphatase activities
PFKFB2
the bifunctional enzyme has 6-phosphofructo-2-kinase and fructose-2,6-biphosphatase activities
PFKFB3
-
PFKFB3
bifunctional enzyme with 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
PFKFB3
the bifunctional enzyme has 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
PFKFB4
bifunctional enzyme with 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
mechanism
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
mechanism
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
kinetic mechanism
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
random mechanism
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities, residues K51, T52, D128, and K172 are key catalytic residues for the 6-phosphofructo-2-kinase activity
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
HBP1 and HBP2 both show a random order equilibrium bi bi mechanism, bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
ordered bi bi mechanism, structural and functional roles of Cys-238 and Cys-295
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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CAS REGISTRY NUMBER
COMMENTARY
78689-77-7
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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
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
-
reverse reaction, at 50% the rate of forward reaction
-
r
CTP + D-fructose 6-phosphate
CDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ITP + beta-D-fructose 6-phosphate
IDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?, r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
activity determined spectrophotometrically by coupling the fructose-1,6-bisphosphate production to the oxidation of NADH
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli, role in the progression of cancerous cells, antiproliferative effects during inhibitor incubation determined
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
transgene causes changes in cardiac metabolite concentrations, increased glycolysis, reduced palmitate oxidation, protection from hypoxia
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
no substrates are diphosphate, glucose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
sugar phosphate specificity
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: ribose 5-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: ribose 5-phosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: 1-O-methyl-D-fructose 6-phosphate, alpha-/beta-methyl-D-fructofuranoside 6-phosphate, 2,5-anhydro-D-mannitol 6-phosphate, D-arabinose 5-phosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
site-directed mutant study and inhibition kinetics suggest that the reaction will be catalyzed most efficiently by the protein when the substrates bind to the active pocket in an ordered manner in which ATP binds first
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
phosphorylation of PFK-2 on Ser-32, inhibition of hepatic glucose metabolism
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?, r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
-
less effective than ATP
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
analysis of MgATP-induced tetramer formation
-
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
-
?
additional information
?
-
-
mechanism of enzyme inhibition by ATP analyzed by structure determination
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
-
?
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
?
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
-
?
additional information
?
-
recombinant human PFKFB4 kinase activity is 4.3-fold greater than its phosphatase activity
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
isotope exchange reaction between ATP and ADP in the absence of fructose 6-phosphate
-
-
?
additional information
?
-
-
isotope exchange reaction between ATP and ADP in the absence of fructose 6-phosphate
-
-
?
additional information
?
-
-
allosteric bifunctional enzyme, not heart
-
-
?
additional information
?
-
-
isotope exchange between fructose 6-phosphate and fructose 2,6-bisphosphate in the absence of adenine nucleotides
-
-
?
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
-
?
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
?
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
-
?
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
?
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
-
?
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AsO43-
Mg2+
phosphate
Mg2+
-
requirement of a Mg2+ ion, besides the one present in the metal-nucleotide complex, for catalysis in the wild-type enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-bromoacetamido)ethyl phosphate
an irreversible inhibitor of PFK-2 in several cancer cell lines
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
-
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
-
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
-
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
AICAR, associated with phosphorylation of PFK-2 on Ser-32, phosphorylation increased of both wild-type and overexpressed PFK-2 protein in hepatocytes
beta-D-fructose 6-phosphate
modeling of beta-D-fructose 6-phosphate as inhibitor
dibutyryl cAMP
slightly inhibits the complex formation between the enzyme and glucokinase
ethyl 1-(6-oxo-1-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)-1,6-dihydropyridazin-4-yl)-1H-1,2,3-triazole-4-carboxylate
-
MgATP
-
inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP
MgNTP
-
strain DF903, substrate inhibition, most effective: MgATP2, at low fructose concentration
N-(1-pyrenil)maleimide
-
complete loss of catalytic activity, but modified enzyme is able to bind beta-D-fructose 6-phosphate, the presence of MgATP2- completely protects the enzyme activity, the modified enzyme elutes as a monomer
phosphate
-
inhibits wild-type and mutant enzym E190Q. E190 contributs to the mechanism of phosphate inhibition in Pfk-2. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
protein kinase A
inactivation via a 7fold increase in Km for fructose 6-phosphate without alteration of Vmax
-
pyrene maleimide
-
incorporation of 2 mol per mol of enzyme subunit, modifiying Cys-238 and Cys-295, leads to rapid inactivation, MgATP2- protects Cys295, modification of Cys238 does not abolish activity
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
the inhibitor causes a rapid induction of apoptosis in transformed cells, has adequate pharmacokinetic properties, suppresses the glucose uptake and growth of Lewis lung carcinomas in syngeneic mice and yields anti-tumor effects in three human xenograft models of cancer in athymic mice that are comparable to FDA-approved chemotherapeutic agents
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
(3PO), small-molecule inhibitor, mixed inhibition mechanism, both competitive and uncompetitive inhibition, suppresses glycolytic flux and is cytostatic to neoplastic cells, inhibits activity of recombinantly expressed PFKFB3
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
the PFKFB3 inhibitor, 3PO, increases p27 protein in Lewis lung carcinoma cells in vitro and in vivo
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
3PO, a weak competitive inhibitor of PFKFB3, reduces the glucose metabolism and proliferation of cancer cells
glucagon
-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
MgATP2-
-
allosteric inhibition, important regulation of in vivo carbohydrate metabolism under gluconeogenic conditions
MgATP2-
-
E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
N-bromoacetylethanolamine
-
repetitive administration affects inhibition of glycolysis and lipid metabolism, causing suppression of body weight gain
N-bromoacetylethanolamine
-
specific active site-directed inactivator of enzyme, in vitro and in vivo
phosphoenolpyruvate
HBP1 and HBP2, the bifunctional enzyme is regulated via inhibition by phosphoenolpyruvate, uncompetitive against ATP, noncompetitive against beta-D-fructose 6-phosphate
phosphoenolpyruvate
-
mixed-type inhibitory effect, phosphorylation enhances sensitivity
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver; liver enzyme
sn-glycerol 3-phosphate
-
75% decrease in activity of liver enzyme but not hepatoma cells
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity; skeletal muscle enzyme is not sensitive to inhibition
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
not: ITP, GTP, UTP, CTP, strain DF905; phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
enzyme structure-activity relationships, screening of a small-molecule library, and design and synthesis of 5-triazolo-2-arylpyridazinone analogus inhibitors, molecular docking using the X-ray structure for human PFKFB3, PDB ID 2AXN, overview
-
additional information
synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
additional information
-
synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
additional information
not inhibited by up to 0.75 mM 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
additional information
-
no inhibition by phosphorylation with Ca2+/calmodulin dependent protein kinase; no inhibition by protein kinase C
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation at lower pH-values; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation of foetal liver enzyme by protein kinase C, but no effect on adult liver cells
-
additional information
-
not: cAMP or protein kinase alone; phosphorylation at pH 6.6, not at pH 8; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of heart and skeletal muscle enzyme
-
additional information
-
loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme. The deletion of 7 N-terminal amino acids causes a 75% decrease in activity; phosphorylation site: Ser-32
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M
-
additional information
-
kinetic of phosphorylation by cAMP-dependent protein kinase
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 80% decrease in activity of the liver cells but not of hepatoma cells; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of kidney, testis and heart enzyme
-
additional information
-
the islet enzyme lacks protein kinase A and C phosphorylation sites
-
additional information
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
no inhibition by lactate, glyceraldehyde 3-phosphate, beta-D-fructose 1,6-bisphosphate
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme
-
additional information
enzyme is not affected by protein kinase C
-
additional information
enzyme is not affected by protein kinase C
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
Insulin
-
activation of transfected heart enzyme in human embryonic kidney 293 cells by inducing the phosphorylation of Ser466 and Ser483, activation is mediated by 3-phosphoinositide-dependent kinase-1, protein kinase B is in vivo not essential, activation is sensitive to LY294002 and wortmannin and insensitive to rapaycin and PD98059
-
Insulin
stimulates glycolysis in the heart by increasing glucose transport and activating H-PFK2 by phosphorylating Ser466 and Ser483 through protein kinase B within the C-terminal regulatory domain. Phosphorylation of Ser466 or Thr475 by protein kinase C does not change the enzyme activity. Phosphorylation at Ser84 possibly counteracts the effects of phosphorylation at the activating C-terminal sites
-
additional information
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in HeLa and in MCF-7 human cells, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
additional information
-
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in HeLa and in MCF-7 human cells, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
additional information
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in primary cardiomyocytes, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
additional information
-
one enzyme form is activated dramatically as result of modification by MgATP during preincubation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Aortic Valve Stenosis
Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes.
Arthritis, Rheumatoid
Inhibition of 6-phosphofructo-2-kinase suppresses fibroblast-like synoviocytes-mediated synovial inflammation and joint destruction in rheumatoid arthritis.
Breast Neoplasms
Inhibition of 6-phosphofructo-2-kinase (PFKFB3) suppresses glucose metabolism and the growth of HER2+ breast cancer.
Breast Neoplasms
Overexpression of miR-206 suppresses glycolysis, proliferation and migration in breast cancer cells via PFKFB3 targeting.
Carcinoma
Wortmannin influences hypoxia-inducible factor-1 alpha expression and glycolysis in esophageal carcinoma cells.
Carcinoma, Hepatocellular
Characterization of the binding sites for [3H]glibenclamide in rat liver membranes.
Carcinoma, Hepatocellular
Glucose response elements in a gene that codes for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
Carcinoma, Hepatocellular
Rat hepatoma (HTC) cell 6-phosphofructo-2-kinase differs from that in liver and can be separated from fructose-2,6-bisphosphatase.
Colonic Neoplasms
Phosphofructokinase 2 and glycolysis in HT29 human colon adenocarcinoma cell line. Regulation by insulin and phorbol esters.
Heart Failure
Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes.
Infections
Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses.
Insulin Resistance
Adipocyte inducible 6-phosphofructo-2-kinase suppresses adipose tissue inflammation and promotes macrophage anti-inflammatory activation.
Insulin Resistance
Disruption of inducible 6-phosphofructo-2-kinase ameliorates diet-induced adiposity but exacerbates systemic insulin resistance and adipose tissue inflammatory response.
Insulin Resistance
Targeted overexpression of inducible 6-phosphofructo-2-kinase in adipose tissue increases fat deposition but protects against diet-induced insulin resistance and inflammatory responses.
Myocardial Ischemia
[Effect of electroacupuncture preconditioning of "Neiguan"(PC6) on myocardial LKB1/AMPK/PFK2 pathway in myocardial ischemia rats].
Neoplasms
Activation of p53 mediated glycolytic inhibition-oxidative stress-apoptosis pathway in Dalton's lymphoma by a ruthenium (II)-complex containing 4-carboxy N-ethylbenzamide.
Neoplasms
An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect.
Neoplasms
GM-CSF Enhances Macrophage Glycolytic Activity In Vitro and Improves Detection of Inflammation In Vivo.
Neoplasms
Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues.
Neoplasms
PFKFB3 gene silencing decreases glycolysis, induces cell-cycle delay and inhibits anchorage-independent growth in HeLa cells.
Neoplasms
Small-molecule inhibition of 6-phosphofructo-2-kinase activity suppresses glycolytic flux and tumor growth.
Neoplasms
Targeted disruption of inducible 6-phosphofructo-2-kinase results in embryonic lethality.
Neoplasms
Targeting 6-phosphofructo-2-kinase (PFKFB3) as a therapeutic strategy against cancer.
Neoplasms
Targeting the sugar metabolism of tumors with a first-in-class 6-phosphofructo-2-kinase (PFKFB4) inhibitor.
Neoplasms
The role of 6-phosphofructo-2-kinase (PFK-2)/fructose 2,6-bisphosphatase (FBPase-2) in metabolic reprogramming of cancer cells.
Neoplasms
Upregulation of 6-phosphofructo-2-kinase (PFKFB3) by hyperactivated mammalian target of rapamycin complex 1 is critical for tumor growth in tuberous sclerosis complex.
pyruvate kinase deficiency
Erythrocyte fructose 2,6-bisphosphate content in congenital hemolytic anemias.
Sarcoma, Avian
Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses.
Sepsis
Hepatic phosphofructokinase-1 activity and fructose 2,6-bisphosphate levels in patients with abdominal sepsis.
Starvation
Changes in rat hepatic fructose 2,6-bisphosphate and 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase activity during three days of consumption of a high protein diet or starvation.
Starvation
Molecular cloning of a cDNA encoding 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from liver of Sparus aurata: nutritional regulation of enzyme expression.
Starvation
Starvation or diabetes decreases the content but not the mRNA of 6-phosphofructo-2-kinase in rat liver.
Tuberous Sclerosis
Upregulation of 6-phosphofructo-2-kinase (PFKFB3) by hyperactivated mammalian target of rapamycin complex 1 is critical for tumor growth in tuberous sclerosis complex.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.048
ATP
-
pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme
0.29 - 0.38
ATP
-
pH 7.1, 30°C, kinetic data of various enzyme forms
0.21
beta-D-fructose 2,6-bisphosphate
-
pH 7.4, 30°C, in presence of phosphate
0.05
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, in presence of phosphate
0.05
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C, MgATP2-, phosphorylated chicken enzyme
0.057
beta-D-fructose 6-phosphate
-
wild-type, 1 mM co-substrate, chosen in order avoid the effect of MgATP binding at the allosteric site to the binding of fructose-6-P to the catalytic site, that is observed above 1 mM MgATP
0.06
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant L307, 1 mM co-substrate
0.062
beta-D-fructose 6-phosphate
-
Y306A, C-terminal point mutant, 1 mM co-substrate
0.008
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged wild-type HBP1
0.013
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged chimeric mutant enzyme, phosphorylated or nonphosphorylated
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, wild-type enzyme, testis
0.02
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant D299, 1 mM co-substrate
0.022
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.025
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, liver, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.029
beta-D-fructose 6-phosphate
-
L307A, C-terminal point mutant, 1 mM co-substrate
1.4
beta-D-fructose 6-phosphate
pH 7.8, 25°C, effect of phosphate on Km
1.4
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, absence of phosphate
0.006
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C and heating at 90°C for 10 min, with ATP, in presence of phosphate
0.031
beta-D-fructose 6-phosphate
-
recombinant wild-type enzyme and mutant C238A
0.036
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.0073
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant H253A
0.056
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme
0.0064
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant S477D
0.0066
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutants T470D and S460D/T470D
0.0074
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged wild-type HBP2
0.0071
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant H253A/S460D
0.0071
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, wild-type HBP1
0.0092
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant Hnon-phosphorylated, is-tagged HBP1 deletion mutant
39
beta-D-fructose 6-phosphate
pH 7.1, 30°C, protein kinase A treated enzyme
0.0095
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged HBP1 mutant S302R
0.0067
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant S460D
0.02 - 0.03
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in presence of phosphate
0.02 - 0.03
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in presence of phosphate
0.156
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, in presence of phosphate
0.5 - 1
beta-D-fructose 6-phosphate
-
pH 8.0, forms 1-3, kinetic data of various enzyme forms
0.33 - 0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C, kinetic data of various enzyme forms
0.019 - 0.021
beta-D-fructose 6-phosphate
-
pH 7.8, in presence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in absence of phosphate
1.9 - 4.6
beta-D-fructose 6-phosphate
pH 7.1, 30°C, recombinant isozyme Tb1
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
comparison of Km of hepatoma cells and liver enzyme
-
additional information
additional information
-
kinetics of native and pyrene maleimide modified enzyme
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
recombinant wild-type and mutant enzymes, Km for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate, kinetics, modeling
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.391
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A
0.394
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D
0.394
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D/T470D
0.399
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 mutant S302R
0.401
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A/S460D
0.405
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S477D
0.407
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type HBP1
0.43
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP1
0.435
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant T470
0.447
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP2
0.654
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
0.678
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.696
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 deletion mutant
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
kcat of wild-type and mutant HBP1 and of HBP2 with beta-D-fructose 2,6-bisphosphate, kcat for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
inhibition of recombinant PFKFB3 protein, no inhibition of purified PFK-1 activity
12.7
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
13
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant T470
9.2
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D
9.5
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A/S460D
9.7
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S477D
8.5
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D/T470D
9.9
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type HBP1
11.8
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP2
12.2
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP1
11.1
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A
9.6
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 deletion mutant
10.9
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 mutant S302R
13.4
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.53
phosphoenolpyruvate
-
noncompetitive to fructose 6-phosphate, pH 7.5, 30°C
additional information
additional information
-
guanidine-inhibition of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of Ki for MgATP2- inhibition at different free Mg2+ concentrations
-
additional information
additional information
-
comparison of Ki of wild type and mutant enzymes
-
additional information
additional information
modeling of inhibition of HBP1 and HBP2 by phosphoenolpyruvate and beta-D-fructose 6-phosphate, Km for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.026
(2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.027
2-hydroxy-4-[(naphthalen-1-ylsulfonyl)amino]benzoic acid
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
3H-benzo[e]indol-2-yl(pyridin-4-yl)methanone
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0084
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0034
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
10
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.011
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0091
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.007
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0087
5-(4-acetyl-5-methyl-1H-1,2,3-triaz