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Information on EC 2.7.1.105 - 6-phosphofructo-2-kinase and Organism(s) Rattus norvegicus and UniProt Accession P07953

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EC Tree
IUBMB Comments
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P07953
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
6-phosphofructo-2-kinase, phosphofructokinase 2, phosphofructokinase-2, upfk-2, inducible 6-phosphofructo-2-kinase, fructose 6-phosphate 2-kinase, ipfk2, tpfk-2, phosphofructokinase-2/fructose bisphosphatase-2, 6-phosphofructose 2-kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2
-
6-phosphofructo-2-kinase
-
-
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
-
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex
-
-
6-phosphofructose 2-kinase
-
-
-
-
ATP:D-fructose-6-phosphate 2-phosphotransferase
-
-
-
-
fructose 6-phosphate 2-kinase
-
-
-
-
kinase, 6-phosphofructo-2-(phosphorylating)
-
-
-
-
PFKFB3
PFKFB4
phosphofructokinase 2
-
-
-
-
phosphofructokinase-2/fructose bisphosphatase-2
-
-
tPFK-2
-
isoform, product of Pfkfb4 gene
uPFK-2
-
isoform, product of Pfkfb3 gene
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
78689-77-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
show the reaction diagram
-
reverse reaction, at 50% the rate of forward reaction
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
ATP + D-psicose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
ATP + D-tagatose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
ATP + L-sorbose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GMP
-
activation
IMP
-
activation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AsO43-
phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dibutyryl cAMP
slightly inhibits the complex formation between the enzyme and glucokinase
2,5-anhydro-D-mannitol 6-phosphate
-
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
AICAR, associated with phosphorylation of PFK-2 on Ser-32, phosphorylation increased of both wild-type and overexpressed PFK-2 protein in hepatocytes
beta-D-fructose 2,6-bisphosphate
citrate
diphosphate
-
-
glucagon
guanidine
-
inactivation, unfolding
m-periodate
-
strong, DTT protects or reverses
N-bromoacetylethanolamine
-
specific active site-directed inactivator of enzyme, in vitro and in vivo
phosphoenolpyruvate
sn-glycerol 3-phosphate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
glucose
-
inhibition by N-bromoacetylethanolamine
iodoacetamide
additional information
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in primary cardiomyocytes, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00087 - 0.4
ATP
0.02
beta-D-fructose 2,6-bisphosphate
-
pH 7.5, 30°C
0.0038 - 1.1
beta-D-fructose 6-phosphate
7.4
D-psicose 6-phosphate
-
pH 7.5, 30°C
15
D-tagatose 6-phosphate
-
pH 7.5, 30°C
0.175
L-Sorbose 6-phosphate
-
pH 7.5, 30°C
0.5
MgATP2-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 0.19
ATP
0.14 - 0.19
beta-D-fructose 6-phosphate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.095
2,5-anhydro-D-mannitol 6-phosphate
-
pH 7.5, 30°C
0.16
ADP
-
pH 6.6, 25°C
0.025 - 0.2
citrate
2
N-bromoacetylethanolamine
-
pH 7.5, 30°C, recombinant testis enzyme
0.014 - 2.3
phosphoenolpyruvate
0.15
sn-glycerol 3-phosphate
-
pH 7.1
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00031
-
skeletal muscle
0.00295
-
heart
0.021
-
liver
0.055
-
adult
0.08
-
foetal
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
in the presence of phosphate
7.3 - 8.4
-
wild-type enzyme
7.5
-
native enzyme, absence of phosphate
7.5 - 8
assay at
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 4.8
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
equal amounts of isozyme L and M
Manually annotated by BRENDA team
-
resembles muscle enzyme
Manually annotated by BRENDA team
-
placenta-type isozyme is expressed in Kupffer cells of the liver
Manually annotated by BRENDA team
-
uPFK-2, tPFK-2
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the glucokinase-PFK2/FBPase2 complex predominately localizes to the cytoplasmic compartment, peripheral location of the glucokinase-PFK2/FBPase2 interaction close to the plasma membrane
Manually annotated by BRENDA team
-
tPFK-2
-
Manually annotated by BRENDA team
-
tPFK-2
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
glucose causes decreased binding of glucokinase to glucokinase regulatory protein, GKRP, translocation from the nucleus and increased binding to 6-phosphofructo 2-kinase/fructose 2,6 bisphosphatase-2 (PFK2/FBPase2) in the cytoplasm, while glucagon causes dissociation of glucokinase from PFK2/FBPase2, concomitant with phosphorylation of PFK2/FBPase2 on Ser32, uptake of glucokinase into the nucleus and increased interaction with GKRP
physiological function
role for phosphofructo 2-kinase/fructose 2,6-bisphosphate (PFK2/FBPase2) as a cytoplasmic binding partner of glucokinase and glucagon-induced uptake of glucokinase to the nucleus
malfunction
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
metabolism
-
glycolytic enzyme is present as testis-specific isoforms, these isoforms are expressed specifically or predominantly in spermatogenic cells, often during the post-meiotic phase, and replace the ubiquitous isozymes that are also present in somatic cells
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F261_RAT
471
0
54763
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
101000
-
high speed sedimentation equilibrium
107000 - 109000
-
equilibrium sedimentation, sedimentation velocity analysis
110000
-
gel filtration
112500
-
gel filtration
54000
-
2 * 54000, SDS-PAGE, amino acid sequence
54760
-
2 * 54760, calculated from amino acid sequence
55000
58000
-
2 * 58000, SDS-PAGE
85000 - 90000
-
gel filtration
89100
-
foetal liver, gel filtration
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop, vapor-diffusion method, crystal structures of PFKFB3/beta,gamma-methylene-adenosine 5'-triphosphate/fructose-6-phosphate and PFKFB3/ADP/phosphoenolpyruvate complexes are determined to 2.7 A and 2.25 A resolution
-
the crystal structure of H256A to a resolution of 2.4 A by molecular replacement
the crystal structure of mutant enzyme, the two subunits in the homodimer are arranged in a head-to-head manner, each monomer consists of independent kinase and phosphatase domains, the kinase domains are in close contact, forming an extended hydrophobic core between them, while the phosphatase domains are essentially independent of one another, enzyme is related to the nucleotide monophosphate kinases, and the catalytic domain of G proteins
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S32A/H258A
mutant unable to be phosphorylated
A44G
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values
A44V
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values
H256A
crystal structure
K172A
-
increase in Km of beta-D-fructose 6-phosphate
K172E
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
K172H
-
increase in Km of MgATP2-
K172R
-
increase in Km of beta-D-fructose 6-phosphate
K51A
-
increase in Km of beta-D-fructose 6-phosphate
K51H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
L148N
-
inactive mutant enzyme
L168A
-
inactive mutant enzyme
L168R
-
mutant enzyme shows 0.2% of wild-type activity
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R136K
-
increase in Km of MgATP2-
R136L
-
increase in Km of beta-D-fructose 6-phosphate
R193H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
R193L
-
increase in Km of beta-D-fructose 6-phosphate
R78H
-
increase in Km of MgATP2-
R78L
-
increase in Km of MgATP2-
R79H
-
increase in Km of MgATP2-
R79L
-
increase in Km of MgATP2-
S32A/H258A
-
site-directed mutagenesis, increased activity and incresaed expression level in recombinant HEK-293 cells compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
-
10 min, pH 7.1, progressive inactivation, phosphate does not protect
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze-thawing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C to 0°C, at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
adipose tissue
-
mutant enzyme
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in human HEK-293 cells via adenovirus transfection system, overexpression of the mutant enzyme highly increase the endogenous level of glycolysis and fructose 2,6-bisphosphate in presence of glucagon
-
mutant expressed in Escherichia coli BL21(DL3)
-
transfection of RINm5F cell
-
wild-type and mutant protein, expression via adenovirus transfection system in hepatocytes
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
maximum expression of Pfkfb3 in cells before puberty, maximum expression of Pfkfb4 in adult cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) on hepatic glucose metabolism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loiseau, A.M.; Rider, M.H.; Hue, L.
Purification and properties of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase from rat hepatoma cells
Biochem. Soc. Trans.
15
384-385
1987
Rattus norvegicus
-
Manually annotated by BRENDA team
El-Maghrabi, M.R.; Correia, J.J.; Heil, P.J.; Pate, T.M.; Cobb, C.E.; Pilkis, S.J.
Tissue distribution, immunoreactivity, and physical properties of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Proc. Natl. Acad. Sci. USA
83
5005-5009
1986
Bos taurus, Canis lupus familiaris, Rattus norvegicus
Manually annotated by BRENDA team
Sakurai, T.; Johnson, J.H.; Uyeda, K.
Islet fructose 6-phosphate, 2-kinase: fructose 2,6-bisphosphatase: isozymic form, expression, and characterization
Biochem. Biophys. Res. Commun.
218
159-163
1996
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Van Schaftingen, E.; Hers, H.G.
Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP
Biochem. Biophys. Res. Commun.
101
1078-1084
1981
Rattus norvegicus
Manually annotated by BRENDA team
El-Maghrabi, M.R.; Claus, T.H.; Pilkis, J.; Pilkis, S.J.
Partial purification of a rat liver enzyme that catalyzes the formation of fructose 2,6-bisphosphate
Biochem. Biophys. Res. Commun.
101
1071-1077
1981
Rattus norvegicus
Manually annotated by BRENDA team
El-Maghrabi, M.R.; Fox, E.; Pilkis, J.; Pilkis, S.J.
Cyclic AMP-dependent phosphorylation of rat liver 6-phosphofructo 2-kinase, fructose 2,6-bisphosphatase
Biochem. Biophys. Res. Commun.
106
794-802
1982
Rattus norvegicus
Manually annotated by BRENDA team
Kretschmer, M.; Hofmann, E.
Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP
Biochem. Biophys. Res. Commun.
124
793-796
1984
Rattus norvegicus
Manually annotated by BRENDA team
Sakakibara, R.; Kitajima, S.; Uyeda, K.
Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and fructose 2,6-bisphosphatase
J. Biol. Chem.
259
41-46
1984
Rattus norvegicus
Manually annotated by BRENDA team
Pilkis, S.J.; Regen, D.M.; Stewart, H.B.; Pilkis, J.; Pate, T.M.; El-Maghrabi, M.R.
Evidence for two catalytic sites on 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Dynamics of substrate exchange and phosphoryl enzyme formation
J. Biol. Chem.
259
949-958
1984
Rattus norvegicus
Manually annotated by BRENDA team
Kitajima, S.; Sakakibara, R.; Uyeda, K.
Kinetic studies of fructose 6-phosphate,2-kinase and fructose 2,6-bisphosphatase
J. Biol. Chem.
259
6896-6903
1984
Rattus norvegicus
Manually annotated by BRENDA team
Laloux, M.; Van Schaftingen, E.; Francois, J.; Hers, H.G.
Phosphate dependency of phosphofructokinase 2
Eur. J. Biochem.
148
155-159
1985
Saccharomyces cerevisiae, Rattus norvegicus, Spinacia oleracea
Manually annotated by BRENDA team
Sakakibara, R.; Tanaka, T.; Uyeda, K.; Richards, E.G.; Thomas, H.
Studies of the structure of fructose-6-phosphate 2-kinase:fructose-2,6-bisphosphatase
Biochemistry
24
6818-6824
1985
Rattus norvegicus
Manually annotated by BRENDA team
Kountz, P.D.; McCain, R.W.; El-Maghrabi, M.R.; Pilkis, S.J.
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase: phosphate dependence and effects of other oxyanions
Arch. Biochem. Biophys.
251
110-113
1986
Rattus norvegicus
-
Manually annotated by BRENDA team
Lively, M.O.; El-Maghrabi, M.R.; Pilkis, J.; D'Angelo, G.; Colosia, A.D.; Ciavola, J.A.; Fraser, B.A.; Pilkis, S.J.
Complete amino acid sequence of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
J. Biol. Chem.
263
839-849
1988
Rattus norvegicus
Manually annotated by BRENDA team
Martn-Sanz, P.; Cascales, M.; Bosc, L.
Characterization of 6-phosphofructo-2-kinase from foetal-rat liver
Biochem. J.
281
457-463
1992
Rattus norvegicus
-
Manually annotated by BRENDA team
Van Schaftingen, E.; Davies, D.R.; Hers, H.G.
Inactivation of phosphofructokinase 2 by cyclic AMP - dependent protein kinase
Biochem. Biophys. Res. Commun.
103
362-368
1981
Rattus norvegicus
Manually annotated by BRENDA team
Kitamura, K.; Uyeda, K.; Kangawa, K.; Matsuo, H.
Purification and characterization of rat skeletal muscle fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
J. Biol. Chem.
264
9799-9806
1989
Rattus norvegicus
Manually annotated by BRENDA team
Pilkis, S.J.; Pilkis, J.; El-Maghrabi, M.R.; Claus, T.H.
The sugar phosphate specificity of rat hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
J. Biol. Chem.
260
7551-7556
1985
Rattus norvegicus
Manually annotated by BRENDA team
Rider, M.H.; Foret, D.; Hue, L.
Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes
Biochem. J.
231
193-196
1985
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Kountz, P.D.; El-Maghrabi, M.R.; Pilkis, S.J.
Isolation and characterization of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from bovine liver
Arch. Biochem. Biophys.
238
531-543
1985
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Rider, M.H.; Vandamme, J.; Lebeau, E.; Vertommen, D.; Vidal, H.; Rousseau, G.G.; Vanderkerkhove, J.; Hue, L.
The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing
Biochem. J.
285
405-411
1992
Bos taurus, Rattus norvegicus
-
Manually annotated by BRENDA team
Kitamura, K.; Uyeda, K.
Purification and characterization of myocardial fructose-6-phosphate,2-kinase and fructose-2,6-bisphosphatase [published erratum appears in J Biol Chem 1989 Jan 25;264(3):1901]
J. Biol. Chem.
263
9027-9033
1988
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Lange, A.J.; Li, L.; Vargas, A.M.; Pilkis, S.J.
Expression of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli. Role of N-2 proline in degradation of the protein
J. Biol. Chem.
268
8078-8084
1993
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Rider, M.H.
Regulation of fructose-2,6-bisphosphate synthesis and breakdown in heart and skeletal muscle
Biochem. Soc. Trans.
15
988-991
1987
Bos taurus, Columba sp., Rattus norvegicus
Manually annotated by BRENDA team
Li, L.; Lange, A.J.; Pilkis, S.J.
Isolation of a cDNA for chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase [published erratum appears in Biochem Biophys Res Commun 1999 Jun 16;259(3):711]
Biochem. Biophys. Res. Commun.
190
397-405
1993
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Rider, M.H.; Hue, L.
Bifunctionality of muscle and heart 6-phosphofructo-2-kinase: skeletal muscle 6-phosphofructo-2-kinase catalyses fructose 2,6-bisphosphate hydrolysis whereas heart 6-phophofructo-2-kinase contains little fructose-2,6-bisphphophatase
Biochem. Soc. Trans.
15
379-380
1987
Rattus norvegicus
-
Manually annotated by BRENDA team
Kurland, I.J.; Chapman, B.; El-Maghrabi, M.R.
N- and C-termini modulate the effects of pH and phosphorylation on hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Biochem. J.
347
459-467
2000
Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Hasemann, C.A.; Istvan, E.S.; Uyeda, K.; Deisenhofer, J.
The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies
Structure
4
1017-1029
1996
Rattus norvegicus
Manually annotated by BRENDA team
Watanabe, F.; Jameson, D.M.; Uyeda, K.
Enzymic and fluorescence studies of four single-tryptophan mutants of rat testis fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase
Protein Sci.
5
904-913
1996
Rattus norvegicus
Manually annotated by BRENDA team
Mizuguchi, H.; Cook, P.F.; Hasemann, C.A.; Uyeda, K.
Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues
Biochemistry
36
8775-8784
1997
Rattus norvegicus
Manually annotated by BRENDA team
Tominaga, N.; Tsujikawa, T.; Minami, Y.; Wu, R.F.; Watanabe, F.; Sakakibara, R.; Uyeda, K.
Effect of replacement of the amino and the carboxyl termini of rat testis fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase with those of the liver and heart isozymes
Arch. Biochem. Biophys.
347
275-281
1997
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Yuen, M.H.; Wang, X.L.; Mizuguchi, H.; Uyeda, K.; Hasemann, C.A.
A switch in the kinase domain of rat testis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Biochemistry
38
12333-12342
1999
Rattus norvegicus (P25114)
Manually annotated by BRENDA team
Sakakibara, R.; Okudaira, T.; Fujiwara, K.; Kato, M.; Hirata, T.; Yamanaka, S.; Naito, M.; Fukasawa, M.
Tissue distribution of placenta-type 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Biochem. Biophys. Res. Commun.
257
177-181
1999
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Harada, Y.; Tominaga, N.; Watanabe, M.; Shimokawa, R.; Ishiguro, M.; Sakakibara, R.
Inhibition of fructose-6-phosphate,2-kinase by N-bromoacetylethanolamine phosphate in vitro and in vivo
J. Biochem.
121
724-730
1997
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Zhu, Z.; Ling, S.; Yang, Q.H.; Li, L.
Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence His444-Arg-Glu-Arg in modulation of the bisphosphatase activity by its kinase domain
Biochem. J.
357
513-520
2001
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Bruni, P.; Vandoolaeghe, P.; Rousseau, G.G.; Hue, L.; Rider, M.H.
Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isozymes in white adipose tissue
Eur. J. Biochem.
259
756-761
1999
Rattus norvegicus
Manually annotated by BRENDA team
Goldstein, B.N.; Maevsky, A.A.
Critical switch of the metabolic fluxes by phosphofructo-2-kinase:fructose-2,6-bisphosphatase. A kinetic model
FEBS Lett.
532
295-299
2002
Rattus norvegicus
Manually annotated by BRENDA team
Payne, V.A.; Arden, C.; Wu, C.; Lange, A.J.; Agius, L.
Dual role of phosphofructokinase-2/fructose bisphosphatase-2 in regulating the compartmentation and expression of glucokinase in hepatocytes
Diabetes
54
1949-1957
2005
Rattus norvegicus
Manually annotated by BRENDA team
Payne, V.A.; Arden, C.; Lange, A.J.; Agius, L.
Contributions of glucokinase and phosphofructokinase-2/fructose bisphosphatase-2 to the elevated glycolysis in hepatocytes from Zucker fa/fa rats
Am. J. Physiol. Regul. Integr. Comp. Physiol.
293
R618-R625
2007
Rattus norvegicus
Manually annotated by BRENDA team
Kim, S.G.; Cavalier, M.; El-Magrabi, M.R.; Lee, Y.M.
A direct substratesubstrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
J. Biol. Chem.
370
14-26
2007
Rattus norvegicus
Manually annotated by BRENDA team
Smith, W.E.; Langer, S.; Wu, C.; Baltrusch, S.; Okar, D.A.
Molecular coordination of hepatic glucose metabolism by the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex
Mol. Endocrinol.
21
1478-1487
2007
Rattus norvegicus
Manually annotated by BRENDA team
Mukhtar, M.H.; Payne, V.A.; Arden, C.; Harbottle, A.; Khan, S.; Lange, A.J.; Agius, L.
Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R766-R774
2008
Rattus norvegicus (Q9JJH5)
Manually annotated by BRENDA team
Mykhalchenko, V.G.; Minchenko, D.O.; Tsuchihara, K.; Moenner, M.; Komisarenko, S.V.; Bikfalvi, A.; Esumi, H.; Minchenko, O.H.
Expression of mouse 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 mRNA alternative splice variants in hypoxia
Ukr. Biokhim. Zh.
80
19-25
2008
Rattus norvegicus (A7UAK3), Mus musculus (A7UAK4), Mus musculus (A7UAK5), Mus musculus (A7UAK6), Mus musculus
Manually annotated by BRENDA team
Gomez, M.; Navarro-Sabate, A.; Manzano, A.; Duran, J.; Obach, M.; Bartrons, R.
Switches in 6-phosphofructo-2-kinase isoenzyme expression during rat sperm maturation
Biochem. Biophys. Res. Commun.
387
330-335
2009
Rattus norvegicus
Manually annotated by BRENDA team
Langer, S.; Kaminski, M.T.; Lenzen, S.; Baltrusch, S.
Endogenous activation of glucokinase by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is glucose dependent
Mol. Endocrinol.
24
1988-1997
2010
Rattus norvegicus
Manually annotated by BRENDA team
Baltrusch, S.; Schmitt, H.; Brix, A.; Langer, S.; Lenzen, S.
Additive activation of glucokinase by the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and the chemical activator LY2121260
Biochem. Pharmacol.
83
1300-1306
2012
Rattus norvegicus
Manually annotated by BRENDA team
Langer, S.; Okar, D.A.; Schultz, J.; Lenzen, S.; Baltrusch, S.
Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation
FEBS Lett.
586
1419-1425
2012
Rattus norvegicus (P07953)
Manually annotated by BRENDA team
Novellasdemunt, L.; Tato, I.; Navarro-Sabate, A.; Ruiz-Meana, M.; Mendez-Lucas, A.; Perales, J.C.; Garcia-Dorado, D.; Ventura, F.; Bartrons, R.; Rosa, J.L.
Akt-dependent activation of the heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) isoenzyme by amino acids
J. Biol. Chem.
288
10640-10651
2013
Homo sapiens (O60825), Homo sapiens, Rattus norvegicus (Q9JJH5), Rattus norvegicus Sprague-Dawley (Q9JJH5)
Manually annotated by BRENDA team
Cullen, K.S.; Al-Oanzi, Z.H.; OHarte, F.P.; Agius, L.; Arden, C.
Glucagon induces translocation of glucokinase from the cytoplasm to the nucleus of hepatocytes by transfer between 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase-2 and the glucokinase regulatory protein
Biochim. Biophys. Acta
1843
1123-1134
2014
Rattus norvegicus (P07953), Rattus norvegicus Wistar (P07953)
Manually annotated by BRENDA team