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Information on EC 3.1.3.46 - fructose-2,6-bisphosphate 2-phosphatase
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EC Tree
3.1.3.46 fructose-2,6-bisphosphate 2-phosphataseIUBMB Comments
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
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Word Map
- 3.1.3.46
- fructose-1,6-bisphosphatase
-
gluconeogenesis
-
gluconeogenic
- amp
- 6-phosphate
-
1,6-bisphosphatase
-
tp53-induced
- phosphoenolpyruvate
- isozyme
- chloroplast
- endothelial
- glycogen
- pentose
- 6-phosphofructo-1-kinase
- hepatocytes
-
carboxykinase
- fructose-6-phosphate
-
hypoxia-inducible
- glucokinase
-
camp-dependent
-
warburg
- pepck
-
3.1.3.11
-
glucose-induced
- g6pase
- spinach
- hk2
-
fructose-1
- hypoglycemia
- glucose-6-phosphatase
- hexokinase
-
fru-6-p
-
glycogenolysis
-
calvin
-
p53-inducible
-
anaphase-promoting
- phosphofructokinase-1
- phosphoenzyme
-
fructose-6-p
- molecular biology
- medicine
- pharmacology
- agriculture
-
pentose-phosphate
-
z-line
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fbpase, pfkfb3, tigar, pfk-2, pfkfb4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, fructose-2,6-bisphosphatase, pfkfb2, pfk-2/fbpase-2, f-2,6-p2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (gene PFKFB3)
-
bifunctional enzyme
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4
D-fructose-2,6-bisphosphatase
-
-
-
-
F2KP
FBPase
FBPase-2
fructose-2,6-bisphosphatase
fructose-2,6-diphosphatase
-
-
-
-
heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Pfk-2
PFK-2/FBPase-2
PFK-2/FDPase-2
PFK2
PFKFB
PFKFB-3
isoform, bifunctional enzyme possessing 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
PFKFB1
PFKFB2
PFKFB3
PFKFB4
phosphatase, fructose 2,6-di-
-
-
-
-
additional information
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
fructose-2,6-bisphosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
-
-
-
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
mechanism
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
Pigeon
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
mechanism, kinetic model
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
mechanism, regulation
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
catalytic phosphorylation of His residues is essential, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
catalytic site structure and interactions involving residues H258, E327, H392, R397, and H446, detailed molecular mechanism and regulation in wild-type and mutant enzymes, overview, catalytic phosphorylation of His residues is essential, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
substrate binding loop structure and regulation mechanism, interactions of enzyme and substrate involve residues K47, R74, R75, R98, and T126, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
beta-D-fructose 2,6-bisphosphate induces a global conformational change in the absence of AMP
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
in-line phosphoryl transfer initiated by a substrate-assisted mechanism
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
the complex of E. coli FBPase with beta-D-fructose 2,6-bisphosphate remains in the R-state with dynamic loops in the engaged conformation
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
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CAS REGISTRY NUMBER
COMMENTARY
81611-75-8
-
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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
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
regulation mechanism, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, isozyme PFKFB3 mediates beta-D-fructose 2,6-bisphosphate production in proliferating cells, isozyme roles in glycolysis regulation in adipocytes, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, which is a major allosteric activator of 6-phosphofructo 1-kinase, a key regulatory enzyme in glycolysis, the minor splice isozyme PFKFB-4 is responsible for hypoxia and dimethyloxalylglycine inhibition
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
substrate binding loop structure, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, isozyme PFKFB3 mediates beta-D-fructose 2,6-bisphosphate production in proliferating cells, isozyme roles in glycolysis regulation in adipocytes, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
fructose 2,6-bisphosphate + H2O
?
-
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
fructose 2-phosphate + phosphate
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
-
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
?
additional information
?
-
-
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
?
additional information
?
-
-
the enzyme is important in degradation of the biological factor beta-D-fructose 2,6-bisphosphate, the bifunctional PFK-2/FDPase-2 shows a metabolic switch to change between the two separate activities, metabolic regulation overview
-
-
?
additional information
?
-
-
catalytic cycle of the catalytic domain of fructose-2 6-biphosphatase, overview, the bifunctional PFK-2/FDPase-2 shows a metabolic switch to change between the two activities, involved in glycolysis and gluconeogenesis, regulation overview
-
-
?
additional information
?
-
-
enzyme expression is highly reduced in diabetic mice, insulin is required for enzyme induction/regulation, a high enzyme expression level reduces blood glucose level and increases the expression of glucokinase, metabolic regulation overview
-
-
?
additional information
?
-
-
PFKFB3 overexpression increases the glycolysis level
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
enzyme involved in regulation of glycolytic flux, role of glycolysis in cell cycle progression
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
-
the enzyme is important in degradation of the biolocical factor beta-D-fructose 2,6-bisphosphate, the bifunctional PFK-2/FDPase-2 shows a metabolic switch to change between the two separate activities, involved in glycolysis and gluconeogenesis, metabolic regulation overview
-
-
?
additional information
?
-
-
catalytic cycle of the catalytic domain of fructose-2 6-biphosphatase, overview
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
?
additional information
?
-
-
activation of glucokinase is endogenously mediated by interaction with the bisphosphatase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase which increases the phosphorylating capacity of glucokinase
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
?
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
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
regulation mechanism, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, isozyme PFKFB3 mediates beta-D-fructose 2,6-bisphosphate production in proliferating cells, isozyme roles in glycolysis regulation in adipocytes, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, which is a major allosteric activator of 6-phosphofructo 1-kinase, a key regulatory enzyme in glycolysis, the minor splice isozyme PFKFB-4 is responsible for hypoxia and dimethyloxalylglycine inhibition
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the bifunctional enzyme is responsible for regulation of intracellular beta-D-fructose 2,6-bisphosphate level, isozyme PFKFB3 mediates beta-D-fructose 2,6-bisphosphate production in proliferating cells, isozyme roles in glycolysis regulation in adipocytes, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
fructose 2,6-bisphosphate + H2O
?
-
-
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
?
additional information
?
-
-
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
?
additional information
?
-
-
the enzyme is important in degradation of the biological factor beta-D-fructose 2,6-bisphosphate, the bifunctional PFK-2/FDPase-2 shows a metabolic switch to change between the two separate activities, metabolic regulation overview
-
-
?
additional information
?
-
-
enzyme expression is highly reduced in diabetic mice, insulin is required for enzyme induction/regulation, a high enzyme expression level reduces blood glucose level and increases the expression of glucokinase, metabolic regulation overview
-
-
?
additional information
?
-
-
PFKFB3 overexpression increases the glycolysis level
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
enzyme involved in regulation of glycolytic flux, role of glycolysis in cell cycle progression
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
study of bifunctional enzyme evolution
-
-
?
additional information
?
-
-
the enzyme is important in degradation of the biolocical factor beta-D-fructose 2,6-bisphosphate, the bifunctional PFK-2/FDPase-2 shows a metabolic switch to change between the two separate activities, involved in glycolysis and gluconeogenesis, metabolic regulation overview
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
?
additional information
?
-
-
the enzyme rather than its substrate fructose 2,6-bisphosphate is crucial in glucose-induced insulin secretion through regulation of glucokinase activity or subcellular targeting
-
-
?
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-2-(1,3-benzodioxol-5-ylmethylidene)butanedioic acid
-
mimics binding pattern of fructose 6-phosphate
([2-[(5-nitropyridin-2-yl)amino]phenyl]sulfanyl)acetic acid
-
mimics binding pattern of fructose 6-phosphate
1,1'-ethane-1,2-diylbis(4-acetylpyrrolidine-2,3,5-trione)
-
mimics binding pattern of fructose 6-phosphate
1-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-(2-methyl-4-nitro-1H-imidazol-1-yl)ethanol
-
mimics binding pattern of fructose 6-phosphate
1-amino-4-(2-nitro-1H-imidazol-1-yl)butan-2-ol
-
mimics binding pattern of fructose 6-phosphate
2-(1,3-benzodioxol-5-ylmethyl)-3-methylbutanedioic acid
-
mimics binding pattern of fructose 6-phosphate
2-(2-nitrophenoxy)-N-phenylacetamide
-
mimics binding pattern of fructose 6-phosphate
2-(3H-indol-7-ylmethyl)butanedioic acid
-
mimics binding pattern of fructose 6-phosphate
2-(5-amino-4-carbamoyl-1H-pyrazol-1-yl)ethanesulfonic acid
-
mimics binding pattern of fructose 6-phosphate
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
-
-
2-(acetylamino)-beta-oxophenylalanine
-
mimics binding pattern of fructose 6-phosphate
2-nitro-N-(pyrazin-2-ylmethyl)benzenesulfonamide
-
mimics binding pattern of fructose 6-phosphate
2-nitro-N-quinolin-3-ylbenzenesulfonamide
-
mimics binding pattern of fructose 6-phosphate
2-[(4-nitro-1H-benzimidazol-7-yl)sulfanyl]ethyl benzoate
-
mimics binding pattern of fructose 6-phosphate
2-[(5-nitropyridin-2-yl)amino]ethyl 5-nitro-1H-pyrrole-2-carboxylate
-
mimics binding pattern of fructose 6-phosphate
2-[(furan-2-ylmethyl)amino]-5-nitrobenzoic acid
-
mimics binding pattern of fructose 6-phosphate
2-[[(2Z)-2-(phenylhydrazono)acetyl]amino]benzoic acid
-
mimics binding pattern of fructose 6-phosphate
2-[[2-(2,4-dinitrophenyl)hydrazino]carbonyl]benzoic acid
-
mimics binding pattern of fructose 6-phosphate
3,3'-(2,4,6-trioxo-1,3,5-triazinane-1,3-diyl)dipropanoic acid
-
mimics binding pattern of fructose 6-phosphate
3-(3-pyridin-2-yl-1,2,4-oxadiazol-5-yl)-N-(tetrahydrofuran-2-ylmethyl)propanamide
-
mimics binding pattern of fructose 6-phosphate
3-acetylphenyl (3-acetylphenyl)acetate
-
mimics binding pattern of fructose 6-phosphate
3-[(2-pyridin-2-ylhydrazino)carbonyl]pyrazine-2-carboxylic acid
-
mimics binding pattern of fructose 6-phosphate
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
-
-
5,6,7,8-tetrahydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
competitive inhibitor
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)-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-hydroxy-N-(4-nitro-1,3-thiazol-2-yl)-2,4-dioxopentanamide
-
mimics binding pattern of fructose 6-phosphate
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
-
-
additional information
-
expression of isozyme PFKFB3 is reduced by treatment of 3T3-L1 cells with insulin
-
additional information
-
inhibitor screening and structure-based docking, overview
-
additional information
-
expression of isozyme PFKFB3 is reduced by prolonged treatment of 3T3-L1 cells with insulin
-
additional information
-
streptozotocin highly reduces enzyme expression, treated mice show undetecable low levels of insulin, the effect is reversible by application of insulin
-
additional information
a significant decrease of isoform PFKFB-4 mRNA expression is found in the lung from rats treated by methyl tretbutyl ether during two months; a significant decrease of isoform PFKFB-4 mRNA expression is found in the lung from rats treated by methyl tretbutyl ether during two months
-
additional information
a significant decrease of isoform PFKFB-4 mRNA expression is found in the lung from rats treated by methyl tretbutyl ether during two months; a significant decrease of isoform PFKFB-4 mRNA expression is found in the lung from rats treated by methyl tretbutyl ether during two months
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
brazilin
-
a component isolated from Caesalpinia sappan wood, increases enzyme activity by increasing the cellular content of fructose-2,6-bishosphate via increased levels of fructose 6-phosphate and hexose 6-phosphate produced by activates 6-phosphofructo-2-kinase and pyruvate kinase, overview
Protein phosphatase 2A
-
cyclic AMP dependent protein kinase inactivation reversible by
-
Cyclic AMP dependent protein kinase
-
catalyzes phosphorylation at a single NH2-terminal residue, Ser-32
-
Protein kinase C
-
phosphorylation requires phosphatidyl serine, Ca2+ and diolein
-
additional information
-
the hepatic enzyme expression is stimulated at transcriptional level by both insulin and glucocorticoids
-
additional information
-
the hepatic enzyme expression is stimulated at transcriptional level by both insulin and glucocorticoids
-
additional information
significant increase of the expression of PFKFB-3 mRNA is observed in the mouse lungs, testes and brain in hypoxia
-
additional information
-
significant increase of the expression of PFKFB-3 mRNA is observed in the mouse lungs, testes and brain in hypoxia
-
additional information
-
the hepatic enzyme expression is stimulated at transcriptional level by both insulin and glucocorticoids, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
Homo sapiens
-
IC50 above 1.0 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.5
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
Homo sapiens
-
IC50 above 0.5 mM,in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.026
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
1
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
Homo sapiens
-
IC50 above 1.0 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
1
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
Homo sapiens
-
IC50 above 1.0 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
1
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
IC50 above 1.0 mM,in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0034
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
10
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
Homo sapiens
-
IC50 above 10 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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
-
IC50 above 0.5 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0087
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0096
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0026
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0074
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.0262
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
1
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
IC50 above 1.0 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.013
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.5
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
Homo sapiens
-
IC50 above 0.5 mM, in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
0.055
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
Homo sapiens
-
in 40 mM Tris pH 7.5, 20 mM MgCl2, 0.1 mg/ml bovine serum albumin, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
additional information
additional information
-
comparison of kinetic properties of isoforms, enzyme regulation by hormones, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase long form; gene Pfrx
SwissProt
brenda
wild type, two mutants with suppressed expression of F2KP, Tos 17 insertion mutant of OsF2KP1, RNAi mutants of OsF2KP2
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-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
SwissProt
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, expressed in yeast
SwissProt
brenda
isoform PFKFB2, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
SwissProt
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
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-
brenda
-
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, six different isoforms
UniProt
brenda
brain/placenta isozyme PFKFB3; genes PFKFB1-4, four isozymes
SwissProt
brenda
isoform PFKFB2, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
SwissProt
brenda
isoform PFKFB3, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
SwissProt
brenda
isoform PFKFB4, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
SwissProt
brenda
PFKFB4 gene, promoter region, and 5' untranslated region, partial sequence; minor splice isozyme PFKFB-4, major isozyme PFKFB-3
SwissProt
brenda
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94932, 94933, 94934, 94935, 94939, 94940, 94941, 94942, 94944, 94945, 94948, 94952, 94955, 640344, 663563, 665854, 684366, 690361, 716226, 721553, 722278, 730008
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-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
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-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme expressed in Mv1Lu cell line
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme expressed in Mv1Lu cells
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, liver and muscle isoform
-
-
brenda
brain isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
brenda
heart isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
brenda
liver isozyme PFKFB1; genes PFKFB1-4, four isozymes
SwissProt
brenda
testis isozyme PFKFB4; genes PFKFB1-4, four isozymes
SwissProt
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
overexpression of isozyme PFKFB-4 in breast and colon malignant tumors compared to non-malignant tissue, overexpression of isozyme PFKFB-4 is correlated with enhanced expression of isozyme PFKFB-3, hypoxia-inducible factor 1alpha, dependent glucose transporter 1, and vascular endothelial growth factor VEGF, overview
brenda
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overexpression of isozyme PFKFB-4 in breast and colon malignant tumors compared to non-malignant tissue, overexpression of isozyme PFKFB-4 is correlated with enhanced expression of isozyme PFKFB-3, hypoxia-inducible factor 1alpha, dependent glucose transporter 1, and vascular endothelial growth factor VEGF, overview
brenda
melanoma cell line, minor splice isozyme PFKFB-4, major isozyme is PFKFB-3, isozyme PFKFB-4 is overexpressed in hypoxic conditions
brenda
minor splice isozyme PFKFB-4, major isozyme is PFKFB-3
brenda
additional information
-
astrocytoma cell, glioblastoma cell and non neoplastic brain tissue
brenda
-
expression is regulated at transcriptional level by both insulin and glucocorticoids
brenda
-
tissue-specific isoform, amino-terminal phosphorylation site, overview
brenda
-
-
94925, 94933, 94934, 94935, 94939, 94940, 94941, 94942, 94944, 94945, 94955, 640344, 649291, 650947, 651270, 665854, 684366, 690361, 721553, 722278
brenda
-
expression is regulated at transcriptional level by both insulin and glucocorticoids
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
-
PFKFB2 and PFKFB3 mRNA is expressed in human islet cells
brenda
additional information
-
PFKFB3 protein level but not mRNA expression is up-regulated in high-grade astrocytomas
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
knockdown of isoform PFKFB4 reduces tumor growth, glucose uptake and beta-D-fructose 2,6-bisphosphate and increases apoptosis
metabolism
physiological function
additional information
metabolism
-
analysis of glucokinase/6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase complex formation, binding and activation of GK by PFK-2/FBPase-2 in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion
metabolism
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flux through phosphofructokinase-1 is controlled by the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 via production/degradation of fructose-2,6-bisphosphate, a potent allosteric activator of phosphofructokinase-1, as well as direct activation of glucokinase due to a protein-protein interaction
physiological function
-
PFKFB2 has a critical role in glucose uptake and glucose-dependent lipid synthesis. Induction of de novo lipid synthesis by androgen requires the transcriptional up-regulation of HK2 and PFKFB2, and phosphorylation of PFKFB2 generated by the PI3K/Akt signalling pathway to supply the source for lipogenesis from glucose in prostate cancer cells
physiological function
-
the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase acts as an endogenous glucokinase activator
physiological function
fructose-2,6-bisphosphate synthesis by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 is required for the glycolytic response to hypoxia and tumor growth
physiological function
-
PFK2/FBPase2 is most helpful to the glucose-sensing capacity of glucokinase in a fasted organism, or in the transition to threshold as glucose is elevated during feeding
physiological function
both a PFKFB3 inhibitor or PFKFB3 silencing by siRNA suppress the basal and the H2O2-induced autophagy concomitantly with the inhibition of AMPK activity. Overexpression of wild-type PFKFB3 promotes H2O2-induced autophagy, but mutant K472/473A, which lost nuclear localizing property, inhibits the autophagic process. The K472/473A mutant stimulates more lactate production, and decreases the activity of AMPK compared to the wild-type
physiological function
overexpression of microRNA miR-26b represses PFKFB3 mRNA and protein levels followed by modulation of the expression of glycolytic components such as LDHA, GLUT-1 and markers of invasion and cell cycle such as MMP-9, MMP-2, cyclin D1 and p27. The binding site for miR-26b is predicted in the 3'-untranslated region of the PFKFB3 gene
physiological function
TIGAR potently inhibits NF-kappaB-dependent gene expression by suppressing the upstream activation of IKKbeta phosphorylation and kinase activation. Inhibition occurs through a direct binding competition between NEMO and TIGAR for association with the linear ubiquitination assembly complex LUBAC. A TIGAR phosphatase activity-deficient mutant is equally effective as wild-type TIGAR in inhibiting NEMO linear ubiquitination. TIGAR knockout mice display enhanced adipose tissue NF-kappaB signaling, and adipocyte-specific overexpression of TIGAR suppresses adipose tissue NF-kappaB signaling
physiological function
Transforming growth factor TGFbeta1 induces isoform PFKFB3 expression and stimulates glycolysis in Panc1 cells. siRNA silencing of PFKFB3 prevents the stimulation of glycolysis and in vitro invasion ability of Panc1 cells by TGFbeta1. PFKFB3 silencing suppresses the TGFbeta1-mediated induction of the Snail protein
physiological function
tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuates cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth
additional information
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androgen stimulates glycolysis for de novo lipid synthesis by increasing the activities of hexokinase 2 and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2, up-regulation of PFKFB2 expression is mediated by the direct binding of ligand-activated androgen receptor to the PFKFB2 promoter
additional information
-
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Show AA Sequence and Transmembrane Helices (212 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
54000
92000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
96000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
-
1* 36600 and 1* 35600 which seems a degradation product of the larger subunit, SDS-PAGE
tetramer
additional information
?
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
-
head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
isoform pattern in brain, skeletal muscle and liver
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
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the bifunctional liver PFK-2/FDPase-2 has an N-terminal and a C-terminal regulatory region flanking the catalytic core domain harbouring both enzyme active sites, overview, the two activities are physically coupled via the tertiary and quarternary structure
additional information
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domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
-
evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview
additional information
head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
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interaction of enzyme with glucokinase, mechanism of posttranslational glucokinase regulation
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
-
the regulatory region His446 is linked with the catalytic site His258 and His392 via Arg397, overview
additional information
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domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
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evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview
additional information
-
evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphorylatiopn of serine and threonine residues, phosphorylation status is regulated physiologically and developmentally
phosphoprotein
-
phosphorylation by proteinkinase A activates bisphosphatase activity or abolishes inhibitory effect of kinase domain
phosphoprotein
-
the enzyme contains a regulatory Ser32 phosphorylation site in each regulatory region, catalytic phosphorylation of His residues is essential, overview
phosphoprotein
-
PI3K/Akt signalling is involved in the phosphorylation of Ser466 and Ser483 of PFKFB2 in LNCaP cells
phosphoprotein
-
phosphorylation of liver enzyme results in a decrease in its kinase activity, while phosphorylation of the cardiac isoform results in an increase in this activity
phosphoprotein
-
amino-terminal phosphorylation site of liver isoform, carboxy-terminal phosphorylation site of heart and brain isoform, regulation by phosphorylation, overview
phosphoprotein
-
phosphorylation by proteinkinase A at S32 results in reduced affinity for fructose-6-phosphate and stimulates bisphosphatase activity
phosphoprotein
-
catalytic phosphorylation of His residues is essential, overview
phosphoprotein
-
the enzyme is phosphorylated at Ser-32 which causes enhancement of the bisphosphatase activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ADP, ADP mimicks the catalytic binding mode of ATP
as hanging drops in vapor diffusion VDX plates with Mg2+, citrate and beta-D-fructose 2,6-bisphosphate
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by the sitting-drop, vapor-diffusion method, crystals of PFKFB D-fructose 6-phosphate complex in the presence of the nonreactive ATP-analogue AMPPCP beta,gamma-methyleneadenosine 5-triphosphate and crystals the inhibitory complex of PFKFB ADP and phosphoenolpyruvate
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in complex with D-fructose 6-phosphate, diphosphate, or AlF4, sitting drop vapor diffusion method, using 100 mM Tris-HCl, pH 7.5, 20-25% (w/v) ethylene glycol, 200-400 mM tartaric acid, 5% (v/v) glycerol, and 12% (w/v) polyethylene glycol 4000
purified recombinant inducible isozyme PFKFB3, 8 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 10 mM sodium phosphate, 0.05 mM EDTA, 5 mM 2-mercaptoethanol, 0.2 mM ADP, 5% glycerol, and 0.2 mM fructose-6-phosphate, sitting drop vapour diffusion method in presence or absence of fructose-2,6-bisphosphate, the protein sample is mixed with an equal volume of mother liquor containing 50 mM Tris-HCl, pH 7.5, 20-25% ethylene glycol, 12% dioxane, 5% glycerol, and 12% PEG 4000, 2-3 weeks, removal of free phosphate from crystals prior to X-ray diffraction structure determination and analysis at 2.1 A resolution
sitting-drop vapor diffusion of the 1:1 mixture of the protein sample with mother liquor of 50 mM Tris-HCl, pH 7.5, 20.35% ethylene glycol, 12% dioxane, 5% glycerol, and 12% polyethylene glycol 4000. Crystals in a size of 0.2 * 0.2 * 0.05 mm grow in 2-3 weeks. Determination of structure at 2.1 A resolution
to 2.0 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ATP analogue AMPPNP, the presence of a gamma-phosphate makes adoption of the catalytic ATP binding mode impossible for AMPPNP, forcing the analogue to bind atypically with concomitant conformational changes to the ATP binding-pocket
as hanging drops in vapor diffusion VDX plates in complex with Mg2+ or Zn2+ and beta-D-fructose 2,6-bisphosphate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H444A/R445A/R447A
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enhances catalytic rate of bisphosphatase activity and abrogates inhibition by kinase domain
P456E/P457A/A458E
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change of chicken sequence to rat sequence, enzyme behaves like rat enzyme
K472/473A
mutant fails to localize in nucleus, mainly localizes in cytoplasm. The mutant inhibits the autophagic process, stimulates lactate production, and decreases the activity of AMPK compared to the wild-type
E327A
H258A
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site-directed mutagenesis, mutation of the strong nucleophile His258 reduces activity compared to the wild-type enzyme
H446A
-
site-directed mutagenesis, the mutation perturbs significantly and specificially the resonances at the catalytic site assigned to His258 and His392 in His-specific multinuclear NMR study, interaction of residue 446 with R397 is disrupted, comparison to the wild-type enzyme, overview
additional information
E327A
-
catalytic site mutation, role in maintaining the structural integrity
E327A
-
site-directed mutagenesis, inactive mutant, can be rescued by formate at pH 7.0, overview
additional information
N-terminal truncation mutants, behave as monomers, show a decrease in the kinase/phosphatase ration by 4-fold, role of N-terminus for subunit assembly and kinetic properties
additional information
-
N-terminal truncation mutants, behave as monomers, show a decrease in the kinase/phosphatase ration by 4-fold, role of N-terminus for subunit assembly and kinetic properties
additional information
-
chimeric enzymes of chicken catalytic core or intact enzyme plus rat C-terminal 25 amino acids show kinetic properties of rat enzyme
additional information
-
truncation of the C-terminus by 25, but not by 20 amino acids enhances catalytic rate of bisphosphatase activity and abrogates inhibition by kinase domain
additional information
-
cardiac expression of kinase-deficient enzyme in amyocyte cell line inhibits glycolysis, promotes hypertrophy, impairs myocyte function, and reduces insulin sensitivity
additional information
-
PFKFB3 overexpression increases the glycolysis level in recombinant COS-7 cells
additional information
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deletion of N- and C-terminal amino acids to define the catalytic core and the phosphorylation site of protein kinase A
additional information
-
expression of bisphosphatase domain results in cells with low content of fructose-2,6-bisphosphate, having a lower energy content and being less sensitive to oxidative stress
additional information
-
overexpression of intact enzyme results in small increase of kinase activity and levels of fructose-1,6-bisphosphate with little effects on cell metabolism, overexpression of bisphosphatase domain results in signifikant decrease in fructose-1,6-bisphosphatase concentration as well as decrease in lactate production and ATP concentration
additional information
-
overexpression of PFK-2/FBPase-2 in MIN6 cells results in increased insulin secretion
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C for 3 months including 100 mM KCl, 0.5 mM dithiothreitol, 20% glycerol and 50 mM Tris-HCl at pH 7.4
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-80C, 20% glycerol, 200 mM KCl, 1 mM dithiothreitol, 20 mM Hepes, pH 7.1
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme, copurification with phosphofructokinase 2
by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography
recombinant His-tagged inducible isozyme PFKFB3 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, after which the tag is cleaved off by thrombin, followed by anion exchange chromatography, to homogeneity
recombinant His-tagged isozymes 1-4 from purified trypomastigotes, by anion exchange and adsorption chromatography, ultrafiltration and dialysis
-
recombinant His6-tagged bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography and anion exchange chromatography with triethylammonium bicarbonate as eluant
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme, isozymes 1-4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged isozymes 1-4 in Escherichia coli
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in hepatocytes by incubation for 2h with increasing titres of adenoviral vectors
-
expression in MIN-6 cell by incubation for 2h with increasing titres of adenoviral vectors
-
expression of His-tagged inducible isozyme PFKFB3 in Escherichia coli strain BL21(DE3)
expression of His6-tagged bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli strain BL21(DE3) pLysS
-
expression of wild-type and mutant PFK-2 in 6-phosphofructo-2-kinase-deficient myocytes
-
for the RNAi construct using the JJ374 vector and Agrobacterium tumefaciens for transformation
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gene PFKFB4, DNA and amino acid sequence determination, expression analysis in DB-1 melanoma cells
genes PFKFB1-4, chromosomal localization of tissue-specific isozymes, phylogenetic analysis, overview, transcriptional control of isozymes, overview
isozyme PFKFB3 from 3T3-L1 adipocytes, expression and splicing analysis, overview, expression as His-tagged enzyme in Escherichia coli, expression of His-tagged enzyme in COS-7 cells
-
KDO-phosphatase knockout, enzyme is encoded by 4 genes, PFKFB1-4, PFKFB3 is activated by mitogenic, inflammatory and hypoxic stimuli
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overexpression in Arabidopsis using the Agrobacterium tumefaciens GV3101 mediated floral dip method, gene knockout mutants and RNAi mutants, overexpression induces increased levels of soluble sugars, declined starch and triose phosphate content, beta-D-fructose 2,6-bisphosphate contributes to the regulation of starch and sucrose levels
-
overexpression in hepatocytes of the wild type enzyme and of the kinase active double mutant S32A/H258A, overexpression of glukokinase and PFK have a synergistic effect on beta-D-fructose 2,6-bisphosphate levels
-
overexpression of hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate using an adenoviral vector
-
phylogenetic analysis
phylogenetic analysis, transcriptional control of isozymes, overview
possible evolution of the proteobacterial gene by horizontal gene transfer from an eukaryote, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
genes PFKFB1-4, chromosomal localization of tissue-specific isozymes, phylogenetic analysis, overview, transcriptional control of isozymes, overview
genes PFKFB1-4, chromosomal localization of tissue-specific isozymes, phylogenetic analysis, overview, transcriptional control of isozymes, overview
phylogenetic analysis, transcriptional control of isozymes, overview
phylogenetic analysis, transcriptional control of isozymes, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
androgen stimulates glycolysis for de novo lipid synthesis by increasing the activities of hexokinase 2 and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2, up-regulation of PFKFB2 expression in LNCaP cells is mediated by the direct binding of ligand-activated androgen receptor to the PFKFB2 promoter. Expression of PFKFB2 gene is increased 3.0fold by treatment with methyltrienolone, i.e. R1881, a synthetic androgen
-
p53 downregulates PFKFB4 expression by binding to its promoter and mediating transcriptional repression via histone deacetylases
the enzyme is induced in hypoxia and upregulated as a consequence of the transcriptional changes orchestrated by the androgen receptor in prostate cancer cells
-
the enzyme isoform PFKFB4 is about 3fold overexpressed in lung adenocarcinoma compared to normal lung tissue. PFKFB4 mRNA and protein expression are also increased by hypoxia
the protein levels are markedly elevated in high-grade astrocytomas relative to low-grade astrocytomas and corresponding non-neoplastic brain tissue, whereas no significant increase of PFKFB3 mRNA is observed in high-grade astrocytomas
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
FK2P in rice is encoded by two genes OsF2KP1 and OsF2KP2, both are involved in the regulation of primary carbon metabolism in rice leaves during the light period
medicine
molecular biology
pharmacology
-
a pharmacophore map is generated and validated to identify inhibitors of the F6PFBPase complex
medicine
-
overexpression of enzyme results in increase of glucokinase activity, interaction of enzyme with glucokinase at concentrations of glucose physiologically relevant for glucokinase activation, possible site for intervention in type 2 diabetes treatment
medicine
-
PFKFB3 is constitutively expressed in human leukemias and solid tumor cells, inhibitors could act as antineoplastic agents
medicine
pharmacological disruption of the PFKFB4 kinase domain may have clinical utility for the treatment of human cancers
medicine
in colonic and bladder cancer cells, additive growth inhibitory effects are seen with phenformin and with an inhibitor of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3. The increased acidification of the culture medium and glucose uptake caused by phenformin is blocked by combined treatment with PFKFB3 inhibitors
medicine
tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of the allosteric regulator fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuated cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth
molecular biology
-
overexpression alone has negligible effects on insulin secretion, only in combination with 6-phosphofructo-2-kinase, partial down-regulation of endogenous PFKFB2 and PFKFB3 in INS1 cells by siRNA decreased PFK-2/FBPase-2 protein, fructose 2,6-bisphosphate content, glucokinase activity and glucose-induced insulin secretion
molecular biology
-
overexpression alone has negligible effects on insulin secretion, only in combination with 6-phosphofructo-2-kinase, partial down-regulation of endogenous PFKFB2 and PFKFB3 in INS1 cells by siRNA decreased PFK-2/FBPase-2 protein, fructose 2,6-bisphosphate content, glucokinase activity and glucose-induced insulin secretion
molecular biology
-
overexpression alone has negligible effects on insulin secretion, only in combination with 6-phosphofructo-2-kinase, partial down-regulation of endogenous PFKFB2 and PFKFB3 in INS1 cells by siRNA decreased PFK-2/FBPase-2 protein, fructose 2,6-bisphosphate content, glucokinase activity and glucose-induced insulin secretion
-
molecular biology
-
overexpression alone has negligible effects on insulin secretion, only in combination with 6-phosphofructo-2-kinase, partial down-regulation of endogenous PFKFB2 and PFKFB3 in INS1 cells by siRNA decreased PFK-2/FBPase-2 protein, fructose 2,6-bisphosphate content, glucokinase activity and glucose-induced insulin secretion
-
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REF.
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TITLE
JOURNAL
VOL.
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YEAR
ORGANISM (UNIPROT)
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Mechanism of the bisphosphatase reaction of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by 1H-15N NMR spectroscopy
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Rattus norvegicus
brenda
Baltrusch, S.; Schmitt, H.; Brix, A.; Langer, S.; Lenzen, S.
Additive activation of glucokinase by the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and the chemical activator LY2121260
Biochem. Pharmacol.
83
1300-1306
2012
Rattus norvegicus
brenda
Langer, S.; Okar, D.A.; Schultz, J.; Lenzen, S.; Baltrusch, S.
Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation
FEBS Lett.
586
1419-1425
2012
Rattus norvegicus
brenda
Brooke, D.G.; van Dam, E.M.; Watts, C.K.; Khoury, A.; Dziadek, M.A.; Brooks, H.; Graham, L.J.; Flanagan, J.U.; Denny, W.A.
Targeting the Warburg Effect in cancer; relationships for 2-arylpyridazinones as inhibitors of the key glycolytic enzyme 6-phosphofructo-2-kinase/2,6-bisphosphatase 3 (PFKFB3)
Bioorg. Med. Chem.
22
1029-1039
2014
Homo sapiens
brenda
Ros, S.; Schulze, A.
Balancing glycolytic flux: the role of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatases in cancer metabolism
Cancer Metab.
1
8-8
2013
Homo sapiens
brenda
Pegoraro, C.; Maczkowiak, F.; Monsoro-Burq, A.H.
Pfkfb (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) isoforms display a tissue-specific and dynamic expression during Xenopus laevis development
Gene Expr. Patterns
13
203-211
2013
Xenopus laevis
brenda
Novellasdemunt, L.; Tato, I.; Navarro-Sabate, A.; Ruiz-Meana, M.; Mendez-Lucas, A.; Perales, J.C.; Garcia-Dorado, D.; Ventura, F.; Bartrons, R.; Rosa, J.L.
Akt-dependent activation of the heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) isoenzyme by amino acids
J. Biol. Chem.
288
10640-10651
2013
Rattus norvegicus, Homo sapiens (O60825), Homo sapiens
brenda
Chesney, J.; Clark, J.; Klarer, A.C.; Imbert-Fernandez, Y.; Lane, A.N.; Telang, S.
Fructose-2,6-bisphosphate synthesis by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (PFKFB4) is required for the glycolytic response to hypoxia and tumor growth
Oncotarget
5
6670-6686
2014
Homo sapiens (Q16877), Homo sapiens
brenda
Merrins, M.J.; Bertram, R.; Sherman, A.; Satin, L.S.
Phosphofructo-2-kinase/fructose-2,6-bisphosphatase modulates oscillations of pancreatic islet metabolism
PLoS ONE
7
e34036
2012
Mus musculus
brenda
Cavalier, M.C.; Kim, S.G.; Neau, D.; Lee, Y.H.
Molecular basis of the fructose-2,6-bisphosphatase reaction of PFKFB3: transition state and the C-terminal function
Proteins
80
1143-1153
2012
Homo sapiens (Q16875), Homo sapiens
brenda
Lea, M.A.; Guzman, Y.; Desbordes, C.
Inhibition of growth by combined treatment with inhibitors of lactate dehydrogenase and either phenformin or inhibitors of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Anticancer Res.
36
1479-1488
2016
Homo sapiens (Q16875)
brenda
Yalcin, A.; Solakoglu, T.H.; Ozcan, S.C.; Guzel, S.; Peker, S.; Celikler, S.; Balaban, B.D.; Sevinc, E.; Gurpinar, Y.; Chesney, J.A.
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase-3 is required for transforming growth factor beta1-enhanced invasion of Panc1 cells invitro
Biochem. Biophys. Res. Commun.
484
687-693
2017
Homo sapiens (Q16875)
brenda
Tang, Y.; Kwon, H.; Neel, B.A.; Kasher-Meron, M.; Pessin, J.B.; Yamada, E.; Pessin, J.E.
The fructose-2,6-bisphosphatase TIGAR suppresses NF-kappaB signaling by directly inhibiting the linear ubiquitin assembly complex LUBAC
J. Biol. Chem.
293
7578-7591
2018
Mus musculus (Q8BZA9)
brenda
Ros, S.; Floeter, J.; Kaymak, I.; Da Costa, C.; Houddane, A.; Dubuis, S.; Griffiths, B.; Mitter, R.; Walz, S.; Blake, S.; Behrens, A.; Brindle, K.M.; Zamboni, N.; Rider, M.H.; Schulze, A.
6-Phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 is essential for p53-null cancer cells
Oncogene
36
3287-3299
2017
Homo sapiens (Q16877)
brenda
Du, J.Y.; Wang, L.F.; Wang, Q.; Yu, L.D.
miR-26b inhibits proliferation, migration, invasion and apoptosis induction via the downregulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 driven glycolysis in osteosarcoma cells
Oncol. Rep.
33
1890-1898
2015
Homo sapiens (Q16875), Homo sapiens
brenda
Yan, S.; Wei, X.; Xu, S.; Sun, H.; Wang, W.; Liu, L.; Jiang, X.; Zhang, Y.; Che, Y.
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoform 3 spatially mediates autophagy through the AMPK signaling pathway
Oncotarget
8
80909-80922
2017
Homo sapiens (Q16875)
brenda
Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding
Proteins
85
117-124
2017
Homo sapiens (O60825), Homo sapiens, Bos taurus (P26285), Bos taurus
brenda
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