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EC Tree
IUBMB Comments The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
The taxonomic range for the selected organisms is: Bos taurus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fbpase, pfkfb3, tigar, pfk-2, pfkfb4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, fructose-2,6-bisphosphatase, pfkfb2, pfk-2/fbpase-2, f-2,6-p2,
more
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
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fructose-2,6-bisphosphatase
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
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D-fructose-2,6-bisphosphatase
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fructose-2,6-bisphosphatase
fructose-2,6-diphosphatase
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phosphatase, fructose 2,6-di-
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fructose-2,6-bisphosphatase
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fructose-2,6-bisphosphatase
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additional information
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
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beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
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beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
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hydrolysis of phosphoric ester
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beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
fructose 2,6-bisphosphate + H2O
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
additional information
?
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
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fructose 2,6-bisphosphate + H2O
fructose 6-phosphate + phosphate
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additional information
?
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
?
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study of bifunctional enzyme evolution
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
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?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
fructose 2,6-bisphosphate + H2O
?
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?
additional information
?
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beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
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?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
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?
additional information
?
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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additional information
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study of bifunctional enzyme evolution
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fructose 6-phosphate
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noncompetetive
N-bromoacetylethanolamine
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Protein kinase C
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phosphorylation requires phosphatidyl serine, Ca2+ and diolein
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0.021
fructose 2,6-bisphosphate
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liver isozyme PFKFB1; genes PFKFB1-4, four isozymes
SwissProt
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isozyme PFKFB1
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isozyme PFKFB3
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brenda
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skeletal
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isozyme PFKFB3
brenda
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brenda
isozyme PFKFB2
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
additional information
tissue-specific expression of the different isozymes, overview
brenda
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brenda
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F261_BOVIN
471
0
54657
Swiss-Prot
other Location (Reliability: 4 )
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100000
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gel filtration or sucrose density gradient centrifugation
53800
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53800, gel electrophoresis
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dimer
homodimeric bifunctional enzyme
dimer
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dimer
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54000-580000, SDS-PAGE
dimer
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53800, gel electrophoresis
dimer
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2 * 50000-55000, SDS-PAGE
dimer
homodimeric bifunctional enzyme
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
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
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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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phylogenetic analysis, transcriptional control of isozymes, overview
phylogenetic analysis, transcriptional control of isozymes, overview
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Taniyama, M.; Kitamura, K.; Thomas, H; Lawson, J.W.R.; Uyeda, K.
Isozymes of fructose 6-phosphate, 2-kinase:fructose-2,6-bisphosphatase in rat and bovine heart, liver, and skeletal muscle
Biochem. Biophys. Res. Commun.
157
949-954
1988
Bos taurus, Rattus norvegicus
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Pilkis, S.J.; Claus, T.H.; Kountz, P.D.; El-Maghrabi, M.R.
Enzymes of the fructose 6-phosphate-fructose 1,6-bisphosphate substrate cycle
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
18
3-46
1987
Bos taurus, Rattus norvegicus
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brenda
Kitamura, K.; Uyeda, K.; Hartman, F.C.; Kangawa, K.; Matsuo, H.
Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase
J. Biol. Chem.
264
6344-6348
1989
Bos taurus, Rattus norvegicus
brenda
Sakata, J.; Abe, Y.; Uyeda, K.
Molecular cloning of the DNA and expression and characterization of rat testes fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase
J. Biol. Chem.
266
15764-15770
1991
Bos taurus
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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
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Rider, M.H.; Bertrand, L.; Vertommen, D.; Michels, P.A.; Rousseau, G.G.; Hue, L.
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
Biochem. J.
381
561-579
2004
Arabidopsis thaliana (Q9MB58), Bos taurus (P26285), Bos taurus (P49872), Bos taurus (Q28901), Desulfovibrio desulfuricans, Drosophila melanogaster (Q9VWH7), Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877), Leishmania major, Mus musculus (P70265), Mus musculus (Q9ESY2), Rattus norvegicus (O35552), Rattus norvegicus (P07953), Rattus norvegicus (P25114), Rattus norvegicus (Q9JJH5), Schizosaccharomyces pombe
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Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding
Proteins
85
117-124
2017
Homo sapiens (O60825), Homo sapiens, Bos taurus (P26285), Bos taurus
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