HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.1.3.46 - fructose-2,6-bisphosphate 2-phosphatase
for references in articles please use BRENDA:EC3.1.3.46Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
Word Map
- 3.1.3.46
- fructose-1,6-bisphosphatase
-
gluconeogenesis
-
gluconeogenic
- insulin
- diabetes
- amp
-
1,6-bisphosphatase
- 6-phosphate
- glycogen
- phosphoenolpyruvate
-
tp53-induced
- chloroplast
- isozyme
- 6-phosphofructo-1-kinase
- fructose-6-phosphate
- pentose
-
autophagy
-
carboxykinase
-
warburg
- pepck
- spinach
-
hypoxia-inducible
-
camp-dependent
- glucokinase
-
3.1.3.11
- phosphofructokinase-2
- g6pase
-
fructose-1
- glucagon
-
glucose-induced
- hypoglycemia
- glucose-6-phosphatase
-
calvin
-
anaphase-promoting
- phosphoenzyme
-
fru-6-p
- hk2
-
glycogenolysis
-
fructose-6-p
-
z-line
-
p53-inducible
-
glucose-starved
-
pentose-phosphate
- molecular biology
- agriculture
- medicine
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
6-phosphofructo-2-kinase/2,6-bisphosphatase 3, 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2 6-biphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (gene PFKFB3), 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2, 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-4, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Q3U3S6
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, regulation
-
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
-
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; 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; 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; 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; 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; 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; 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; 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; 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; 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
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
-
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
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
81611-75-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
-
-
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
Q9MB58
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P26285, P49872, Q28901
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
Q9VWH7
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Q16875
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Q16877
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O60825
-
-
-
?
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
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P16118
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
Q16877
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
P70265, Q9ESY2
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P70265, Q9ESY2
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
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O35552, P07953, P25114, Q9JJH5
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
?
-
Q9MB58
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9VWH7
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P16118
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
?
-
O35552
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P07953
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P25114
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9JJH5
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Q3U3S6
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
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
-
-
brenda
-
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, six different isoforms
Q9BQU3
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
-
640344, 663563, 665854, 684366, 690361, 716226, 721553, 722278, 730008, 94925, 94932, 94933, 94934, 94935, 94939, 94940, 94941, 94942, 94944, 94945, 94948, 94952, 94955
-
-
brenda
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
expression is regulated at transcriptional level by both insulin and glucocorticoids
brenda
-
-
640344, 649291, 650947, 651270, 665854, 684366, 690361, 701360, 721553, 722278, 94925, 94927, 94933, 94934, 94935, 94939, 94940, 94941, 94942, 94944, 94945, 94955
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; 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; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
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
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
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
-
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
additional information
-
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
additional information
-
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
Show AA Sequence and Transmembrane Helices (203 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
92000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
96000
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
100000
110000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
-
x * 54000, there are 2 isoforms of 54000 and 58000 Da, SDS-PAGE; x * 58000, there are 2 isoforms of 54000 and 58000 Da, SDS-PAGE
dimer
homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme