Information on EC 3.1.3.46 - fructose-2,6-bisphosphate 2-phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.3.46
-
RECOMMENDED NAME
GeneOntology No.
fructose-2,6-bisphosphate 2-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
mechanism, regulation
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
mechanism, kinetic model
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
mechanism
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
catalytic phosphorylation of His residues is essential, overview
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
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
Q9SP17
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
P26285, P49872, Q28901
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
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
Q9VWH7
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
O60825, P16118, Q16875, Q16877
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
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
P70265, Q9ESY2
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
O35552, P07953, P25114, Q9JJH5
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
substrate binding loop structure and regulation mechanism, interactions of enzyme and substrate involve residues K47, R74, R75, R98, and T126, overview
P16118
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
in-line phosphoryl transfer initiated by a substrate-assisted mechanism
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
Pigeon
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
O81398
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
show the reaction diagram
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
Mus musculus C57/BL6, Rattus norvegicus Wistar
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
Mus musculus C57/BL6
-
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
Rattus norvegicus Wistar
-
-
-
6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Q9SP17
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
P26285, P49872, Q28901
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Q9VWH7
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
O60825, P16118, Q16875
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Q16877
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
P70265, Q9ESY2
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
O35552, P07953, P25114, Q9JJH5
-
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 2
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3
Q3U3S6
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4
Q16877
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-4
B0ZTI0, P25114
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphate
-
-
6PF2K/Fru-2,6-P2ase
-
-
D-fructose-2,6-bisphosphatase
-
-
-
-
F-2,6-P2
-
-
F2KP
-
-
FBPase-2
Q9SP17
-
FBPase-2
P26285, P49872, Q28901
-
FBPase-2
Q9VWH7
-
FBPase-2
-
-
FBPase-2
O60825, P16118, Q16875, Q16877
-
FBPase-2
-
-
FBPase-2
-
-
FBPase-2
P70265, Q9ESY2
-
FBPase-2
Mus musculus C57/BL6
-
-
-
FBPase-2
-
-
FBPase-2
O35552, P07953, P25114, Q9JJH5
-
FBPase-2
Rattus norvegicus Wistar
-
-
-
fructose-2,6-bisphosphatase
-
-
-
-
fructose-2,6-bisphosphatase
Q9SP17
-
fructose-2,6-bisphosphatase
P26285, P49872, Q28901
-
fructose-2,6-bisphosphatase
-
-
fructose-2,6-bisphosphatase
Q9VWH7
-
fructose-2,6-bisphosphatase
-
-
fructose-2,6-bisphosphatase
O60825, P16118, Q16875, Q16877
-
fructose-2,6-bisphosphatase
-
-
fructose-2,6-bisphosphatase
P70265, Q9ESY2
-
fructose-2,6-bisphosphatase
O35552, P07953, P25114, Q9JJH5
-
fructose-2,6-bisphosphatase
-
-
fructose-2,6-bisphosphatase
-
-
fructose-2,6-diphosphatase
-
-
-
-
OsF2KP1
-
gene
OsF2KP2
-
gene
Pfk-2
-
-
PFK-2/FBPase
-
-
PFK-2/FBPase-2
Q9SP17
-
PFK-2/FBPase-2
P26285, P49872, Q28901
-
PFK-2/FBPase-2
-
-
PFK-2/FBPase-2
Q9VWH7
-
PFK-2/FBPase-2
-
-
PFK-2/FBPase-2
O60825, P16118, Q16875, Q16877
-
PFK-2/FBPase-2
-
-
PFK-2/FBPase-2
P70265, Q9ESY2
-
PFK-2/FBPase-2
-
-
PFK-2/FBPase-2
O35552, P07953, P25114, Q9JJH5
-
PFK-2/FBPase-2
-
-
PFK-2/FBPase-2
-
-
PFK-2/Fru-2,6-P2
-
-
PFK2
-
bifunctional enzyme
PFKFB
Q16877
-
PFKFB
-
-
PFKFB-3
Q3U3S6
isoform, bifunctional enzyme possessing 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities
PFKFB-4
B0ZTI0, P25114
isoform, bifunctional enzyme
PFKFB1
-
gene
PFKFB1
-
gene
PFKFB1
Mus musculus C57/BL6
-
gene
-
PFKFB1
-
gene
PFKFB1
Rattus norvegicus Wistar
-
gene
-
PFKFB2
-
-
PFKFB2
-
gene
PFKFB2
-
gene
PFKFB2
Mus musculus C57/BL6
-
gene
-
PFKFB2
-
gene
PFKFB2
Rattus norvegicus Wistar
-
gene
-
PFKFB3
-
gene
PFKFB3
Mus musculus C57/BL6
-
gene
-
PFKFB3
-
gene
PFKFB3
Rattus norvegicus Wistar
-
gene
-
PFKFB4
-
gene
phosphatase, fructose 2,6-di-
-
-
-
-
RH2K
Q9JJH5
-
additional information
Q9SP17
bifunctional enzyme, cf. EC 2.7.1.105
additional information
P26285, P49872, Q28901
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
Q9VWH7
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
O60825, P16118, Q16875
bifunctional enzyme, cf. EC 2.7.1.105
additional information
Q16877
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
cf. EC 2.7.1.105
additional information
P70265, Q9ESY2
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
cf. EC 2.7.1.105
additional information
O35552, P07953, P25114, Q9JJH5
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
additional information
-
bifunctional enzyme, cf. EC 2.7.1.105
CAS REGISTRY NUMBER
COMMENTARY
81611-75-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
Q9SP17
SwissProt
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Uniprot
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, expressed in yeast
Uniprot
Manually annotated by BRENDA team
cv. Columbia and heterozygous mutant line F2KP-KO
-
-
Manually annotated by BRENDA team
brain isozyme PFKFB3; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
heart isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
liver isozyme PFKFB1; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase long form; gene Pfrx
SwissProt
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, six different isoforms
UniProt
Manually annotated by BRENDA team
bifunctional enzyme
-
-
Manually annotated by BRENDA team
brain/placenta isozyme PFKFB3; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
heart isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
isozymes PFKFB-4 and PFKFB-3
-
-
Manually annotated by BRENDA team
isozymes PFKFB1-4
-
-
Manually annotated by BRENDA team
isozymes PFKFB1-4; recombinant
SwissProt
Manually annotated by BRENDA team
liver isozyme PFKFB1; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
PFKFB4 gene, promoter region, and 5' untranslated region, partial sequence; minor splice isozyme PFKFB-4, major isozyme PFKFB-3
SwissProt
Manually annotated by BRENDA team
testis isozyme PFKFB4; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
This UniProt-ID has been deleted
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
Manually annotated by BRENDA team
C57/BL6
-
-
Manually annotated by BRENDA team
heart isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
inducible isozyme PFKFB3; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
male 129J mice
-
-
Manually annotated by BRENDA team
male and female mice
-
-
Manually annotated by BRENDA team
male C57BL7& mice, isozyme PFKFB3
-
-
Manually annotated by BRENDA team
Mus musculus C57/BL6
C57/BL6
-
-
Manually annotated by BRENDA team
wild type, two mutants with suppressed expression of F2KP, Tos 17 insertion mutant of OsF2KP1, RNAi mutants of OsF2KP2
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme expressed in Mv1Lu cell line
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme expressed in Mv1Lu cells
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, liver and muscle isoform
-
-
Manually annotated by BRENDA team
brain isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
heart isozyme PFKFB2; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
insulin-resistant Zucker fa/fa and Fa/? strains
-
-
Manually annotated by BRENDA team
liver isozyme PFKFB1; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
splice variant
UniProt
Manually annotated by BRENDA team
splice variant
SwissProt
Manually annotated by BRENDA team
testis isozyme PFKFB4; genes PFKFB1-4, four isozymes
SwissProt
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme
SwissProt
Manually annotated by BRENDA team
stock 427, isozymes 1-4
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q9SP17
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
B0ZTI0, P25114
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P70265, Q9ESY2
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q9VWH7
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P70265, Q9ESY2
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P70265, Q9ESY2
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P16118
regulation mechanism, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
P16118
substrate binding loop structure, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Mus musculus C57/BL6, Rattus norvegicus Wistar
-
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q9MB58
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O64983, -
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
P07953
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
O81398
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
Pigeon
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
show the reaction diagram
-
-
fructose 2-phosphate + phosphate
?
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
P07953
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
O81398
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
Pigeon
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme involved in regulation of glycolytic flux, role of glycolysis in cell cycle progression
-
?
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
?
-
P16118
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
-
additional information
?
-
-
metabolic regulation, overview
-
-
-
additional information
?
-
-
PFKFB3 overexpression increases the glycolysis level
-
-
-
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9SP17
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
O60825, P16118, Q16875, Q16877
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
O35552, P07953, P25114, Q9JJH5
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P26285, P49872, Q28901
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P70265, Q9ESY2
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9VWH7
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 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
-
-
-
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
?
-
-
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
?
-
Mus musculus C57/BL6, Rattus norvegicus Wistar
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q9SP17
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q9VWH7
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P70265, Q9ESY2
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P26285, P49872, Q28901
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P70265, Q9ESY2
metabolic regulation of isozyme PFKFB3
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O60825, P16118, Q16875, Q16877
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
O35552, P07953, P25114, Q9JJH5
metabolic regulation of isozyme PFKFB4
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
P16118
regulation mechanism, overview
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
P07953
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
O81398
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
Pigeon
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
fructose 2,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme involved in regulation of glycolytic flux, role of glycolysis in cell cycle progression
-
?
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
?
-
P16118
inducible isozyme PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways, overview
-
-
-
additional information
?
-
-
metabolic regulation, overview
-
-
-
additional information
?
-
-
PFKFB3 overexpression increases the glycolysis level
-
-
-
additional information
?
-
-
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9SP17
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
O60825, P16118, Q16875, Q16877
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
O35552, P07953, P25114, Q9JJH5
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P26285, P49872, Q28901
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
P70265, Q9ESY2
study of bifunctional enzyme evolution
-
-
-
additional information
?
-
Q9VWH7
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 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
?
-
-
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
?
-
Mus musculus C57/BL6, Rattus norvegicus Wistar
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can replace Mg2+
Mg2+
-
dependent on
Mg2+
-
stimulates in the presence of triphosphonucleotides
Mn2+
-
can replace Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
2,5-anhydro-D-mannitol 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-(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
5-hydroxy-N-(4-nitro-1,3-thiazol-2-yl)-2,4-dioxopentanamide
-
mimics binding pattern of fructose 6-phosphate
6-phospho-gluconate
-
-
6-phosphogluconate
Q9MB58
-
AMP
-
beta-D-fructose 2,6-bisphosphate has no effect on AMP inhibition
AMP
-
beta-D-fructose 2,6-bisphosphate enhances AMP inhibition
citrate
-
inhibits the cardiac enzyme
Cyclic AMP dependent protein kinase
-
causes inactivation
-
D-fructose 6-phosphate
O64983, -
mixed type
D-fructose 6-phosphate
-
-
D-fructose-1,6-bisphosphate
Q9MB58
-
D-fructose-6-phosphate
Q9MB58
-
D-glucose-1,6-bisphosphate
Q9MB58
-
D-psicose 6-phosphate
-
poor inhibitor
D-ribose 5-phosphate
-
poor inhibitor
D-tagatose 6-phosphate
-
poor inhibitor
diethyldicarbonate
-
inactivation
dimethyloxalylglycine
Q16877
inhibits the splice isozyme PFKFB-4
F-
-
in presence of glycerol 3-or 2-phosphate
fructose 6-phosphate
-
noncompetetive
fructose 6-phosphate
-
-
fructose 6-phosphate
-
noncompetetive
fructose 6-phosphate
-
-
fructose 6-phosphate
-
-
fructose 6-phosphate
-
-
fructose 6-phosphate
-
-
glycerol 1-phosphate
-
inhibition at low substrate concentrations
glycerol 1-phosphate
-
inhibits at subsaturating substrate concentrations
Insulin
-
opposes action of glucagon or epinephrine
-
L-Sorbose 6-phosphate
-
-
N-Bromoacetylethanolamine
-
-
p-mercuribenzoate
-
-
phosphate
Q9MB58
-
phosphate
O64983, -
uncompetitive
phosphate
-
-
phosphate
-
inhibition at low substrate concentrations
phosphate
-
-
phosphate
-
inhibits at subsaturating substrate concentrations
phosphoenolpyruvate
-
-
Tolbutamide
-
-
vanadate
-
50% inhibition at 0.15 mM
additional information
Q9MB58
not inhibitory: diphosphate
-
additional information
-
expression of isozyme PFKFB3 is reduced by treatment of 3T3-L1 cells with insulin
-
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
B0ZTI0, P25114
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
-
inhibitor screening and structure-based docking, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-phosphoglycerate
-
-
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
Cyclic AMP dependent protein kinase
-
activation
-
Cyclic AMP dependent protein kinase
-
activation
-
Cyclic AMP dependent protein kinase
-
catalyzes phosphorylation at a single NH2-terminal residue, Ser-32
-
Cyclic AMP dependent protein kinase
-
-
-
Cyclic AMP dependent protein kinase
-
-
-
Cyclic AMP dependent protein kinase
-
-
-
dihydroxyacetone phosphate
-
-
epinephrine
-
-
formate
-
activates, interacts with Glu327
glycerol 1-phosphate
-
counteracts fructose 6-phosphate inhibition
glycerol 1-phosphate
-
stimulates
glycerol 1-phosphate
-
activation at high substrate concentrations
glycerol 1-phosphate
-
activates at saturating substrate concentrations
glycerol 1-phosphate
-
counteracts fructose 6-phosphate inhibition
glycerol 1-phosphate
-
-
glycerol 1-phosphate
-
-
Glycerol 2-phosphate
-
-
Glycerol 2-phosphate
-
-
phosphate
-
activates at high substrate concentrations
phosphate
-
activates at saturating substrate concentrations
phosphate
-
counteracts inhibition by fructose-6-phosphate
phosphate
-
-
phosphoenolpyruvate
-
-
Protein kinase C
-
phosphorylation requires phosphatidyl serine, Ca2+ and diolein
-
Protein kinase C
-
-
-
Protein phosphatase 2A
-
cyclic AMP dependent protein kinase inactivation reversible by
-
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, overview
-
additional information
-
insulin highly induces the enzyme expression
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0102
-
beta-D-fructose 2,6-bisphosphate
-
wild type enzyme
0.038
-
beta-D-fructose 2,6-bisphosphate
-
A144G mutant
0.204
-
beta-D-fructose 2,6-bisphosphate
-
A144V mutant
0.00013
-
D-fructose 2,6-bisphosphate
-
pH 7.4
2.8e-05
-
D-fructose-1,6-bisphosphate
Q9MB58
pH 6.0, 25C
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0001
-
fructose 2,6-bisphosphate
-
-
0.0003
-
fructose 2,6-bisphosphate
-
-
0.0003
-
fructose 2,6-bisphosphate
-
-
0.0004
-
fructose 2,6-bisphosphate
-
-
0.0006
-
fructose 2,6-bisphosphate
-
-
0.002
-
fructose 2,6-bisphosphate
-
-
0.0043
-
fructose 2,6-bisphosphate
-
-
0.013
-
fructose 2,6-bisphosphate
-
-
0.016
-
fructose 2,6-bisphosphate
-
-
0.02
-
fructose 2,6-bisphosphate
-
-
0.021
-
fructose 2,6-bisphosphate
-
-
0.032
-
fructose 2,6-bisphosphate
-
-
0.25
-
fructose 2,6-bisphosphate
-
-
0.36
-
fructose 2,6-bisphosphate
-
in presence of 3-phosphoglycerate
0.38
-
fructose 2,6-bisphosphate
-
-
1.4
-
fructose 2,6-bisphosphate
-
in presence of phosphate
additional information
-
additional information
-
kinetic analysis
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
fructose 2,6-bisphosphate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
6-phosphogluconate
Q9MB58
-
9.7
-
D-fructose 6-phosphate
-
pH 7.4
0.08
-
D-fructose-1,6-bisphosphate
Q9MB58
-
0.1
-
D-fructose-6-phosphate
Q9MB58
-
0.85
-
D-glucose-1,6-bisphosphate
Q9MB58
-
0.5
-
phosphate
Q9MB58
-
0.15
-
vanadate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.1e-05
-
-
hepatocyte
1.4e-05
-
-
hepatocyte treated with brazilin
1650
-
O64983, -
phosphatase activity
additional information
-
-
comparison of kinetic properties of isoforms, enzyme regulation by hormones, overview
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
pretreatment with MgATP2-, form 1
7
-
-
-
7.5
-
-
assay at
7.6
-
-
pretreatment with MgATP2-, form 2
8
-
-
assay at
additional information
-
-
pH-dependence of kinetic parameters
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9.29
-
-
amino acid sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
adipocyte cell line
Manually annotated by BRENDA team
-
inducible expression of isozyme PFKFB3, visceral fat cell
Manually annotated by BRENDA team
-
inducible expression of isozyme PFKFB3
Manually annotated by BRENDA team
Q9BQU3
isoform pattern
Manually annotated by BRENDA team
-
tissue-specific isoform, overview
Manually annotated by BRENDA team
P26285, P49872, Q28901
isozyme PFKFB3
Manually annotated by BRENDA team
O60825, P16118, Q16875, Q16877
isozyme PFKFB3
Manually annotated by BRENDA team
O35552, P07953, P25114, Q9JJH5
specific isozyme PFKFB2
Manually annotated by BRENDA team
-
astrocytoma cell, glioblastoma cell and non neoplastic brain tissue
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q16877
melanoma cell line, minor splice isozyme PFKFB-4, major isozyme is PFKFB-3, isozyme PFKFB-4 is overexpressed in hypoxic conditions
Manually annotated by BRENDA team
-
epididymal, reduced expression of isozyme PFKFB3
Manually annotated by BRENDA team
-
tissue-specific isoform, overview
Manually annotated by BRENDA team
P26285, P49872, Q28901
isozyme PFKFB2
Manually annotated by BRENDA team
O60825, P16118, Q16875, Q16877
isozyme PFKFB2
Manually annotated by BRENDA team
P70265, Q9ESY2
isozyme PFKFB2
Manually annotated by BRENDA team
O35552, P07953, P25114, Q9JJH5
specific isozyme PFKFB2
Manually annotated by BRENDA team
-
cardiac isoform
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-, Q9MB58
rosette leaf
Manually annotated by BRENDA team
-
isoform with proteinkinase A phosphorylation site
Manually annotated by BRENDA team
Q9BQU3
isoform pattern
Manually annotated by BRENDA team
-
tissue-specific isoform, amino-terminal phosphorylation site, overview
Manually annotated by BRENDA team
-
expression is regulated at transcriptional level by both insulin and glucocorticoids
Manually annotated by BRENDA team
P26285, P49872, Q28901
isozyme PFKFB1
Manually annotated by BRENDA team
O35552, P07953, P25114, Q9JJH5
specific isozyme PFKFB1
Manually annotated by BRENDA team
-
enzyme expression level determination
Manually annotated by BRENDA team
-
isozyme PFKFB1
Manually annotated by BRENDA team
Q16877
minor splice isozyme PFKFB-4, major isozyme is PFKFB-3
Manually annotated by BRENDA team
-
isoform lacks proteinkinase A phosphorylation site
Manually annotated by BRENDA team
-
tissue-specific isoform, overview
Manually annotated by BRENDA team
-
skeletal
Manually annotated by BRENDA team
-
breast
Manually annotated by BRENDA team
Mus musculus C57/BL6, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
P26285, P49872, Q28901
isozyme PFKFB3
Manually annotated by BRENDA team
O60825, P16118, Q16875, Q16877
isozyme PFKFB3
Manually annotated by BRENDA team
P70265, Q9ESY2
inducible isozyme PFKFB3
Manually annotated by BRENDA team
O35552, P07953, P25114, Q9JJH5
specific isozyme PFKFB2
Manually annotated by BRENDA team
Q9BQU3
isoform pattern
Manually annotated by BRENDA team
-
tissue-specific isoform, overview
Manually annotated by BRENDA team
O60825, P16118, Q16875, Q16877
specific isozyme PFKFB4
Manually annotated by BRENDA team
O35552, P07953, P25114, Q9JJH5
specific isozyme PFKFB4
Manually annotated by BRENDA team
P16118
isozyme PFKFB4
Manually annotated by BRENDA team
-
bloodstream form, grown in rats
Manually annotated by BRENDA team
Mus musculus C57/BL6
-
-
-
Manually annotated by BRENDA team
additional information
P26285, P49872, Q28901
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
Manually annotated by BRENDA team
additional information
O60825, P16118, Q16875, Q16877
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
Manually annotated by BRENDA team
additional information
P70265, Q9ESY2
tissue-specific expression of the different isozymes, overview; tissue-specific expression of the different isozymes, overview
Manually annotated by BRENDA team
additional information
O35552, P07953, P25114, Q9JJH5
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
Manually annotated by BRENDA team
additional information
-
PFKFB2 and PFKFB3 mRNA is expressed in human islet cells
Manually annotated by BRENDA team
additional information
-
PFKFB3 protein level but not mRNA expression is up-regulated in high-grade astrocytomas
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12000
-
-
gel filtration
76200
-
-
gel filtration
100000
-
-
gel filtration or sucrose density gradient centrifugation
100000
-
-
gel filtration
100000
-
-
gel filtration
107000
-
-
equilibrium sedimentation
110000
-
-
gel filtration
110000
-
-
-
140000
-
-
isozyme 2, gel filtration
320000
-
O64983, -
gel filtration
370000
-
Q9MB58
gel filtration
600000
-
-
about, isozyme 1, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q9MB58
x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE
?
-
x * 57078, amino acid sequence calculation
dimer
Q9SP17
homodimeric bifunctional enzyme
dimer
P26285, P49872, Q28901
homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme
dimer
-
homodimeric bifunctional enzyme
dimer
Q9VWH7
homodimeric bifunctional enzyme
dimer
O60825, P16118, Q16875, Q16877
homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme
dimer
-
homodimeric bifunctional enzyme
dimer
P70265, Q9ESY2
homodimeric bifunctional enzyme; homodimeric bifunctional enzyme
dimer
O35552, P07953, P25114, Q9JJH5
homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme; homodimeric bifunctional enzyme
dimer
-
homodimeric bifunctional enzyme
dimer
-
2 * 33000, SDS-PAGE
dimer
-
54000-580000, SDS-PAGE
dimer
-
2 * 56000
dimer
-
2 * 50000-55000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
Pigeon
-
2 * 53000, SDS-PAGE
dimer
-
2 * 50000-55000, SDS-PAGE
dimer
-
-
dimer
-
2 * 55000, gel electrophoresis
dimer
-
53800, gel electrophoresis
dimer
-
54000-580000, SDS-PAGE
dimer
-
53900-55800, SDS-PAGE
dimer
-
53300, SDS-PAGE
homodimer
-
2 * 48000-58000, overview
tetramer
Q9MB58
4 * 83000, deduced from gene sequence
tetramer
O64983, -
4 * 90800, SDS-PAGE
monomer
-
1* 36600 and 1* 35600 which seems a degradation product of the larger subunit, SDS-PAGE
additional information
Q9BQU3
isoform pattern in brain, skeletal muscle and liver
additional information
-
interaction of enzyme with glucokinase, mechanism of posttranslational glucokinase regulation
additional information
-
evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview
additional information
-
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
-
the regulatory region His446 is linked with the catalytic site His258 and His392 via Arg397, overview
additional information
Q9SP17
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
P26285, P49872, Q28901
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; 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
Q9VWH7
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
O60825, P16118, Q16875, Q16877
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; 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
P70265, Q9ESY2
head-to-head structure of the two subunits of the bifunctional enzyme, overview; head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
O35552, P07953, P25114, Q9JJH5
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview; 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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domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-, Q9MB58
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
-
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
as hanging drops in vapor diffusion VDX plates with Mg2+, citrate and beta-D-fructose 2,6-bisphosphate
-
-
P16118
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
-
crystal structure of the liver enzyme
-
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
P16118
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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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
Q9MB58
10 min, inactivation, phosphate protects
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C
-
-80C, 20% glycerol, 200 mM KCl, 1 mM dithiothreitol, 20 mM Hepes, pH 7.1
-
-70C 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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-70C, 20 mM sodium phosphate buffer, pH 7.3, 1 mM dithiothreitol
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-20C, 20% glycerol
-
-80C, 10% glycerol, more than 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by Sephadex G-25 column chromatography
-
by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography
-
bifunctional enzyme, copurification with phosphofructokinase 2
-
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
P16118
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
-
using Ni-NTA affinity columns
-
partially from liver
-
bifunctional enzyme, copurification with phosphofructokinase 2
Pigeon
-
5600fold
-
copurification with phosphofructokinase 2
-
two isoenzymes
-
10000fold
-
two isoenzymes, partially purified
-
by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography
-
recombinant His-tagged isozymes 1-4 from purified trypomastigotes, by anion exchange and adsorption chromatography, ultrafiltration and dialysis
-
15fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
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phylogenetic analysis
Q9SP17
phylogenetic analysis, transcriptional control of isozymes, overview; phylogenetic analysis, transcriptional control of isozymes, overview; phylogenetic analysis, transcriptional control of isozymes, overview
P26285, P49872, Q28901
possible evolution of the proteobacterial gene by horizontal gene transfer from an eukaryote, phylogenetic analysis
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phylogenetic analysis
Q9VWH7
as selenomethionine-substituted protein
-
expression in Escherichia coli
-
expression of His-tagged inducible isozyme PFKFB3 in Escherichia coli strain BL21(DE3)
P16118
expression of His6-tagged bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli strain BL21(DE3) pLysS
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gene PFKFB4, DNA and amino acid sequence determination, expression analysis in DB-1 melanoma cells
Q16877
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; 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
O60825, P16118, Q16875, Q16877
KDO-phosphatase knockout, enzyme is encoded by 4 genes, PFKFB1-4, PFKFB3 is activated by mitogenic, inflammatory and hypoxic stimuli
-
overexpression in Escherichia coli as His6-tagged fusion protein
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DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
phylogenetic analysis
-
expression in MIN-6 cell by incubation for 2h with increasing titres of adenoviral vectors
-
expression of wild-type and mutant PFK-2 in 6-phosphofructo-2-kinase-deficient myocytes
-
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
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overexpression of hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate using an adenoviral vector
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phylogenetic analysis, transcriptional control of isozymes, overview; phylogenetic analysis, transcriptional control of isozymes, overview
P70265, Q9ESY2
for the RNAi construct using the JJ374 vector and Agrobacterium tumefaciens for transformation
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expressed in Mus musculus cardiac cells
-
expression in Escherichia coli
-
expression in hepatocytes by incubation for 2h with increasing titres of adenoviral vectors
-
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; 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
O35552, P07953, P25114, Q9JJH5
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 PFK-2/FBPase-2 in MIN6 cells
-
phylogenetic analysis
-
expression in Escherichia coli
O81398
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
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DNA and amino acid sequence determination and analysis, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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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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
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
P456E/P457A/A458E
-
change of chicken sequence to rat sequence, enzyme behaves like rat enzyme
A44G
-
site directed mutagenesis
A44V
-
site directed mutagenesis
K168A
-
site directed mutagenesis
K168N
-
site directed mutagenesis
E325A
-
role of E325 as acid-base during reaction
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
H258A
-
site-directed mutagenesis, mutation of the strong nucleophile His258 reduces activity compared to the wild-type enzyme
additional information
Q9MB58
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
H444A/R445A/R447A
-
enhances catalytic rate of bisphosphatase activity and abrogates inhibition by kinase domain
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
-
chimeric enzymes of chicken catalytic core or intact enzyme plus rat C-terminal 25 amino acids show kinetic properties of rat enzyme
K168R
-
site directed mutagenesis
additional information
-
PFKFB3 overexpression increases the glycolysis level in recombinant COS-7 cells
additional information
-
cardiac expression of kinase-deficient enzyme in amyocyte cell line inhibits glycolysis, promotes hypertrophy, impairs myocyte function, and reduces insulin sensitivity
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
-
deletion of N- and C-terminal amino acids to define the catalytic core and the phosphorylation site of protein kinase A
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
-
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 PFK-2/FBPase-2 in MIN6 cells results in increased insulin secretion
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
PFKFB3 is constitutively expressed in human leukemias and solid tumor cells, inhibitors could act as antineoplastic agents
medicine
-
the enzyme is a target for cancer chemotherapy
pharmacology
-
a pharmacophore map is generated and validated to identify inhibitors of the F6PFBPase complex
medicine
-
enzyme regulation by hormones, overview
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
Mus musculus C57/BL6
-
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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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
-
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
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
Rattus norvegicus Wistar
-
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
-