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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.
The taxonomic range for the selected organisms is: Bos taurus 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
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6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
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6-phosphofructose 2-kinase
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ATP:D-fructose-6-phosphate 2-phosphotransferase
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fructose 6-phosphate 2-kinase
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kinase, 6-phosphofructo-2-(phosphorylating)
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phosphofructokinase 2
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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phospho group transfer
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ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
MgATP2- + beta-D-fructose 6-phosphate
?
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-
-
?
additional information
?
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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with discrete catalytic sites
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?
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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responsible for regulation of fructose 2,6-bisphosphate-concentration
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?
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Mg2+
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citrate
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citrate
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heart enzyme is more sensitive than liver enzyme
citrate
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at physiological concentrations
phosphoenolpyruvate
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phosphoenolpyruvate
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not
sn-glycerol 3-phosphate
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not
sn-glycerol 3-phosphate
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i.e. alpha-glycerol phosphate
sn-glycerol 3-phosphate
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heart enzyme is less sensitive than liver
additional information
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additional information
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phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
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additional information
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phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
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additional information
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phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
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additional information
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no inhibition by protein kinase C
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additional information
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rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
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additional information
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rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
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Insulin
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activation of transfected heart enzyme in human embryonic kidney 293 cells by inducing the phosphorylation of Ser466 and Ser483, activation is mediated by 3-phosphoinositide-dependent kinase-1, protein kinase B is in vivo not essential, activation is sensitive to LY294002 and wortmannin and insensitive to rapaycin and PD98059
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0.023 - 0.07
beta-D-fructose 6-phosphate
0.0095 - 0.012
MgATP2-
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pH 7.5, 30°C
additional information
additional information
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comparison of Km of wild-type and mutant enzyme
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0.055
ATP
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pH 7.1, 30°C
0.083
ATP
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pH 7.5, 25°C, heart
0.1
ATP
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pH 7.5, 30°C, MgATP
0.023
beta-D-fructose 6-phosphate
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pH 7.5, 25°C, heart
0.023
beta-D-fructose 6-phosphate
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comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.027
beta-D-fructose 6-phosphate
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pH 7.1, 30°C
0.05
beta-D-fructose 6-phosphate
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pH 7.5, 30°C
0.07
beta-D-fructose 6-phosphate
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pH 7.5, 30°C
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additional information
additional information
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comparison of kcat/Km values of wild-type and mutant enzymes
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0.1
phosphoenolpyruvate
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pH 7.5, 30°C, heart
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additional information
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6
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of 54000 Da and 58000 Da isozymes
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7.3 - 9.5
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about half-maximal activity at pH 7.3 and 9.5
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isoform PFKFB2, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
SwissProt
brenda
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cortex
brenda
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brenda
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brenda
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two isozymic forms
brenda
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2 isozymes: result of alternative splitting of the same primary transcript
brenda
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F262_BOVIN
531
0
60811
Swiss-Prot
other Location (Reliability: 2 )
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120000
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2 * 120000, SDS-PAGE
49000
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2 * 49000, SDS-PAGE
52000
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2 * 52000, SDS-PAGE
61000
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x * 61000, SDS-PAGE
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dimer
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dimer
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2 * 49000, SDS-PAGE
dimer
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2 * 120000, SDS-PAGE
dimer
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2 * 52000, SDS-PAGE
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
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phosphoprotein
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phosphoprotein
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phosphorylation site
phosphoprotein
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MW 58000 enzyme form
phosphoprotein
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brain enzyme is phosphorylated, but not activated
phosphoprotein
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phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
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rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
phosphoprotein
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phosphorylation by protein kinase C causes activation
phosphoprotein
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phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
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rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
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to 1.8 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ADP, ADP mimicks the catalytic binding mode of ATP
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S466E
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mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme in vitro
S466E/S483E
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the double mutant is not phosphorylated by protein kinase B, mutation decreases Km of beta-D-fructose 6-phosphate in vitro
S483E
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mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme and mutation decreases citrate inhibition in vitro
additional information
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mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
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wild-type and mutant enzyme
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wild-type enzyme, S466E and S466E/S483E mutants are expressed in Escherichia coli BL21(DE3)pLysE and S483E mutant is expressed in BL21(DE3)pLysS, human embryonic kidney 293 cells are transiently transfected with vectors expressing wild-type heart enzyme
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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
brenda
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
brenda
Sakata, J.; Uyeda, K.
Characterization of two isozymic forms of heart fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase
Biochem. Biophys. Res. Commun.
180
470-474
1991
Bos taurus
brenda
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
brenda
Sakata, J.; Uyeda, K.
Bovine heart fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase: complete amino acid sequence and localization of phosphorylation sites
Proc. Natl. Acad. Sci. USA
87
4951-4955
1990
Bos taurus
brenda
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
brenda
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
-
brenda
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
brenda
Ventura, F.; Rosa, J.L.; Ambrosio, S.; Pilkis, S.J.; Bartrons, R.
Bovine brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Evidence for a neural-specific isozyme
J. Biol. Chem.
267
17939-17943
1992
Bos taurus
brenda
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
brenda
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
brenda
Bertrand, L.; Alessi, D.R.; Deprez, J.; Deak, M.; Viaene, E.; Rider, M.H.; Hue, L.
Heart 6-phosphofructo-2-kinase activation by insulin results from Ser-466 and Ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase B
J. Biol. Chem.
274
30927-30933
1999
Bos taurus
brenda
Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding
Proteins
85
117-124
2017
Homo sapiens (O60825), Bos taurus (P26285)
brenda