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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: Geobacillus stearothermophilus 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-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
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phosphofructokinase 1
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phosphohexokinase
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ATP + beta-D-fructofuranose 6-phosphate = ADP + beta-D-fructofuranose 1,6-bisphosphate
mechanism
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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
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
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?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
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?
UTP + D-fructose 6-phosphate
UDP + 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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?
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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35fold lower reverse reaction velocity
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r
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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
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phosphoenolpyruvate
I153V mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
additional information
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product inhibition of reverse reaction
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GDP
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activation at low concetrations, inhibition above 1 mM
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100 - 129
D-fructose 6-phosphate
0.023 - 0.15
D-fructose 6-phosphate
additional information
additional information
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kinetic study
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100
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I153V
110
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I150V
126
D-fructose 6-phosphate
pH 8.0, 25°C, wild-type enzyme
129
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I234V
0.07
ATP
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pH 8.2, 30°C
0.12
ATP
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pH 8.2, 30°C, native PFK
0.13
ATP
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pH 8.2, 30°C, G212V mutant PFK
0.023
D-fructose 6-phosphate
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pH 8.2, 30°C, native PFK
0.026
D-fructose 6-phosphate
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pH 8.2, 30°C, G212V mutant PFK
0.028
D-fructose 6-phosphate
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pH 8.2, 30°C, cosubstrate GTP
0.03
D-fructose 6-phosphate
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pH 8.2, 30°C, at fructose 6-phosphate concentrations that are less than approx. one-third the fixed MgATP concentration
0.068
D-fructose 6-phosphate
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pH 8.2, 30°C, cosubstrate UTP
0.15
D-fructose 6-phosphate
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pH 8.2, 30°C, cosubstrate CTP
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3.2
fructose 1,6-bisphosphate
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reverse raction, recombinant enzyme
112 - 149
fructose 6-phosphate
112
fructose 6-phosphate
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forward reaction, recombinant enzyme
126
fructose 6-phosphate
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pH 8.2, 30°C, G212V mutant PFK
149
fructose 6-phosphate
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pH 8.2, 30°C, native PFK
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UniProt
brenda
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PFKA_GEOSE
319
0
34119
Swiss-Prot
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homotetramer
x-ray crystallography
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hanging drop vapor diffusion method, using 0.2 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 18% (w/v) polyethylene glycol 8000, at 16°C
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I150V
Km-value for D-fructose 6-phosphate is 1.1fold lower than the wild-type value
I153V
mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
I234V
Km-value for D-fructose 6-phosphate is comparable to the wild-type value
K90/91E
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surface charge-tag substitution, no change in Km for ATP and K1/2 for fructose 6-phosphate
R162E
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single active site substitution, affinity for fructose 6-phosphate is diminished approx. 3 orders of magnitude relative to that of the wild-type
R211E/K213E
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allosteric site substitutions
G212V
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G212V
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inhibition by phosphoenolpyruvate can not be reversed by GDP or ADP, neither ADP nor GDP bind well to the effector site
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-20°C, in 100 mM Tris-HCl buffer, pH 7.4, 1 mM dithiothreitol, 50% glycerol, stable
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Mimetic Blue 1 column chromatography and Mono Q column chromatography
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expressed in Escherichia coli RL257 cells
expression in Escherichia coli
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expression of wild-type and G212V mutant PFK in Escherichia coli
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Byrnes, M.; Zhu, X.; Younathan, E.S.; Chang, S.H.
Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme
Biochemistry
33
3424-3431
1994
Geobacillus stearothermophilus
brenda
Shirakihara, Y.; Evans, P.R.
Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
J. Mol. Biol.
204
973-994
1988
Geobacillus stearothermophilus, Escherichia coli, Escherichia coli DF1020
brenda
Zhu, X.; Byrnes, M.; Nelson, J.W.; Chang, S.H.
Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus
Biochemistry
34
2560-2565
1995
Geobacillus stearothermophilus
brenda
Kimmel, J.L.; Reinhart, G.D.
Isolation of an individual allosteric interaction in tetrameric phosphofructokinase from Bacillus stearothermophilus
Biochemistry
40
11623-11629
2001
Geobacillus stearothermophilus
brenda
Mosser, R.; Reddy, M.; Bruning, J.; Sacchettini, J.; Reinhart, G.
Structure of the apo form of Bacillus stearothermophilus phosphofructokinase
Biochemistry
51
769-775
2012
Geobacillus stearothermophilus (P00512), Geobacillus stearothermophilus
brenda
Whitaker, A.; Reinhart, G.
The effect of introducing small cavities on the allosteric inhibition of phosphofructokinase from Bacillus stearothermophilus
Arch. Biochem. Biophys.
607
1-6
2016
Geobacillus stearothermophilus (P00512), Geobacillus stearothermophilus
brenda