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EC Tree
IUBMB Comments The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
The taxonomic range for the selected organisms is: Dictyostelium discoideum The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phosphofructokinase, 6-phosphofructokinase, 6-phosphofructo-1-kinase, pfk-1, phosphofructokinase-1, pfk-m, phosphofructokinase 1, atp-dependent phosphofructokinase, atp-pfk, pfk-l,
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6-phosphofructo-1-kinase
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6-phosphofructokinase, platelet type
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6-phosphofructose 1-kinase
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6-phosphofructose-1-kinase
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ATP-dependent phosphofructokinase
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D-fructose-6-phosphate 1-phosphotransferase
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fructose 6-phosphate kinase
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fructose 6-phosphokinase
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kinase, phosphofructo- (phosphorylating)
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nucleotide triphosphate-dependent phosphofructokinase
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phospho-1,6-fructokinase
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phosphofructokinase 1
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phosphohexokinase
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PFK
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phosphofructokinase
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phospho group transfer
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ATP:D-fructose-6-phosphate 1-phosphotransferase
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
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ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
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?
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ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
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?
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Mg2+
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required for activity
Mg2+
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MgATP is the active substrate
Mg2+
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most effective ion
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citrate
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strong inhibition
D-fructose 1,6-bisphosphate
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D-Fructose 1-phosphate
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additional information
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not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
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additional information
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not inhibited by ATP
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additional information
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not activated by D-fructose 2,6-bisphosphate
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0.017
ATP
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wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
additional information
additional information
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kinetic data of various organism
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236
ATP
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wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
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brenda
PFK mRNA, PFK protein levels and PFK activity slowly decrease during development
SwissProt
brenda
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brenda
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brenda
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PFKA_DICDI
834
0
92235
Swiss-Prot
other Location (Reliability: 1 )
Q8T8M1_DICDI
97
0
10571
TrEMBL
other Location (Reliability: 1 )
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92400
x * 92400, deduced from nucleotide sequence
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?
x * 92400, deduced from nucleotide sequence
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side-chain modification
2 putative cAMP-dependent protein kinase phosphorylation sites at Ser 293 and Ser 559
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10% (w/v) PEG precipitation, DE52 column chromatography, Blue-Sepharose column chromatography, phosphocellulose column chromatography, and Superdex 200 gel filtration
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expressed in pfk-deficient Saccharomyces cerevisiae strain HD152-1D
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expression in Escherichia coli
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Bloxham, D.P.; Lardy, H.A.
Phosphofructokinase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
8
239-278
1973
Klebsiella aerogenes, Arthrobacter crystallopoietes, Glutamicibacter nicotianae, Bos taurus, Brassica oleracea var. gemmifera, Saccharomyces cerevisiae, Gallus gallus, Clostridium pasteurianum, Oryctolagus cuniculus, Daucus carota, Dictyostelium discoideum, Escherichia coli, Fasciola hepatica, Thermus thermophilus, Ovis aries, Homo sapiens, Lactiplantibacillus plantarum, Lacticaseibacillus casei, Mus musculus, Neurospora crassa, Pisum sativum, Rattus norvegicus, Zea mays
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brenda
Jagannatha Rao, G.S.; Cook, P.F.; Harris, B.G.
Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated
Arch. Biochem. Biophys.
365
335-343
1999
Dictyostelium discoideum (P90521)
brenda
Martinez-Costa, O.; Sanchez, V.; Lzaro, A.; Hernandez, E.; Tornheim, K.; Aragon, J.
Distinct functional roles of the two terminal halves of eukaryotic phosphofructokinase
Biochem. J.
445
213-218
2012
Dictyostelium discoideum, Homo sapiens
brenda