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Aldolase
-
about 120% activity in the presence of 0.005 mM aldolase
-
cAMP-dependent protein kinase
-
Cl-
-
200 mM, 3.1fold activation of cytosolic PFK
D-fructose 1,6-bisphosphate
D-fructose 2,6-bisphosphate
D-fructose-1,6-bisphosphate
-
activates synergistically with AMP and ADP
D-Glucose 1,6-bisphosphate
D-glucose 6-phosphate
-
4.8 mM, 1.5fold increase in activity at 2 mM fructose 6-phosphate, 2fold increase at 4 mM fructose 6-phosphate, in vitro
Dimethylsulfoxide
-
20%, 9fold increase in activity, probably due to crowding effect
fructose 2,6-bisphosphate
-
at near-physiological substrate concentrations, PFK activity requires activators of which the combination of AMP and fructose 2,6-bisphosphate is most efficient as a result of synergistic effects
fructose 6-phosphate
S0.5 value for wild-type 0.88 mM, in presence of 1 mM AMP S0.5 value 0.052 mM. S0.5 value for N-terminal truncation mutant 0.089 mM, in presence of 1 mM AMP S0.5 value 0.030 mM
glycerol
-
40%, 4fold increase in activity, probably due to crowding effect
HAsO42-
-
50 mM, 2.9fold activation of cytosolic PFK
HCO3-
-
200 mM, 2.1fold activation of cytosolic PFK
MgATP2-
the apparent Km for MgATP2- is 0.022 mM
NO3-
-
50 mM 1.6fold activation of cytosolic PFK
phosphoenol pyruvate
slightly enhances activity
Polyethylene glycol
-
20%, 8fold increase in activity, probably due to crowding effect
serotonin
-
stimulates 6-phosphofructo-1-kinase from skeletal muscle via phospholipase C. The activation of phospholipase C in skeletal muscle leads to the recruitment of protein kinase C PKC and calmodulin and the stimulation of calmodulin kinase II, which associates with 6-phosphofructo-1-kinase upon serotonin action
Sodium acetate
-
about 115% activity in the presence of 0.04 mM sodium acetate
ADP
-
activation
ADP
-
at high fructose 6-phosphate concentration, inhibits at low fructose 6-phosphate concentration
ADP
activates at low concentrations, but slightly inhibits at higher concentrations
ADP
-
allosterically activated by both GDP and ADP
ADP
-
1.8 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
AMP
-
activation
AMP
-
activation at low fructose 6-phosphate concentrations, inhibition at high fructose 6-phosphate concentrations
AMP
activates 85000 Da native enzyme form and the 49000 Da shorter fragment
AMP
-
synergistic with fructose 2,6-bisphosphate
AMP
-
one of three most potent activators
AMP
-
2-5 mM, maximal activation at 3 mM ATP
AMP
0.5 mM, 10fold activation of reaction with D-fructose 1,6-bisphosphate and ADP
AMP
-
concomitant with NH4+ and phosphate
AMP
-
activation follows a saturation function, Km: 0.56 mM
AMP
-
at near-physiological substrate concentrations, PFK activity requires activators of which the combination of AMP and fructose 2,6-bisphosphate is most efficient as a result of synergistic effects
AMP
-
0.64 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
AMP
0.5 mM, 2fold activation of reaction with D-fructose 1,6-bisphosphate and ADP
AMP
0.5 mM, 2fold activation of reaction with D-fructose 1,6-bisphosphate and ADP
Calmodulin
-
clotrimazole-inhibited enzyme can be activated by calmodulin
Calmodulin
-
binding of one calmodulin per monomer promotes the dimerization of the enzyme although maintaining its full catalytic activity, 30 nM calmodulin activates 6-phosphofructo-1-kinase in the presence of its inhibitors citrate and lactate
cAMP
-
0.1 mM, activates
cAMP
-
0.1 mM, approx. 5fold activation
cAMP
-
0.4 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
cAMP-dependent protein kinase
-
activation by phosphorylation
-
cAMP-dependent protein kinase
-
kinetics, one of three most potent activators
-
citrate
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
citrate
-
stimulation, by chelating of free Mg2+
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation of flight muscle PFK in the absence of fructose 2,6-bisphosphate
D-fructose 1,6-bisphosphate
-
half-maximal activation at 0.0035 mM
D-fructose 1,6-bisphosphate
-
activation of PFK in INS-1 cell extract
D-fructose 2,6-bisphosphate
the active 49 kDa PFK1 fragment is activated to a higher level by D-fructose 2,6-bisphosphate with respect to the native enzyme, a significant boost in the enzyme activity of the fragment is registered at 1 mM ATP after the introduction of 0.004 mM of D-fructose-2,6-bisphosphate
D-fructose 2,6-bisphosphate
-
activates at concentrations above 0.002 mM
D-fructose 2,6-bisphosphate
-
synergistic with AMP
D-fructose 2,6-bisphosphate
-
3fold activation in the presence of approx. 0.003 mM, i.e. the physiological fructose 2,6-bisphosphate concentration
D-fructose 2,6-bisphosphate
activates
D-fructose 2,6-bisphosphate
-
activation of native and phosphorylated PFK, one of three most potent activators
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
approx. 200-400 mM, maximal activation at 3 mM ATP
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
strong stimulation of mammary gland PFK, Kact: 0.00005 mM
D-fructose 2,6-bisphosphate
-
activation
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
half-maximal activation at 0.0003 mM
D-fructose 2,6-bisphosphate
-
activation
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
activation of PFK in INS-1 cell extract
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
strong positive allosteric action on PFK
D-fructose 2,6-bisphosphate
-
cooperative activation, Km: 0.00023 mM
D-fructose 2,6-bisphosphate
-
converts saturation curves for D-fructose 6-phosphate to hyperbolic and activates PFK synergistically with AMP
D-fructose 2,6-bisphosphate
-
activates
D-Glucose 1,6-bisphosphate
-
-
D-Glucose 1,6-bisphosphate
-
activation only in the presence of AMP
D-Glucose 1,6-bisphosphate
-
activation
D-Glucose 1,6-bisphosphate
-
activation
D-Glucose 1,6-bisphosphate
-
0.02 mM, 474% and 360% activation of M- and L-type PFK, respectively
D-Glucose 1,6-bisphosphate
-
half-maximal activation at 0.013 mM
GDP
-
-
GDP
-
activation at low concetrations, inhibition above 1 mM
GDP
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
GDP
-
allosterically activated by both GDP and ADP
NH4+
-
-
NH4+
-
at very low concentration, kinetics, Km-value: 0.56 mM
NH4+
-
NH4+ increases the affinity for fructose 6-phosphate, counteracts the inhibition by ATP
NH4+
-
required for activity
NH4+
-
40 mM, 50% activation at pH 8.0 and pH 7.2
NH4+
-
concomitant with AMP and phosphate
NH4+
-
required for activity
NH4+
-
activation of muscle enzyme, inhibitory at high concentrations
NH4+
-
increases maximum activity of PFK and the affinity of PFK to fructose 6-phosphate
NH4+
-
activation at low concentrations
NH4+
-
cytosolic isozyme is not activated
phosphate
-
concomitant with NH4+ and AMP
phosphate
-
kinetics, Km-value: 1.64 mM
phosphate
-
concomitant with NH4+ and AMP
phosphate
-
activation of cytosolic and plastidic isoenzyme
phosphate
Dunaliella marina
-
kinetics
phosphate
Dunaliella marina
-
the enzyme is both activated and inhibited by phosphate, depending on fructose 6-phosphate/phosphate-ratio
phosphate
-
concomitant with NH4+ and AMP
phosphate
-
25% activation at 5 mM, inhibition above
phosphate
-
1 mM, strong activtion of plastid PFK at pH-values below 7.0
phosphate
-
cytosolic isozyme: slight activation
phosphate
-
synergistic with AMP
phosphate
-
25 mM, 3.2fold activation of cytosolic PFK
SO42-
-
stimulation
SO42-
-
kinetics, Km-value: 1.73 mM
SO42-
-
50 mM, 2.6fold activation of cytosolic PFK
additional information
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effector studies at near-physiological conditions
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additional information
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not activated by 2-oxoglutarate
-
additional information
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not activated by D-fructose 2,6-bisphosphate
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additional information
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-
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additional information
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addition of oestradiol increases enzyme activity in intact cells
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additional information
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ascites tumor PFK is not activated by fructose-1,6-bisphosphate
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additional information
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allosteric enzyme
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additional information
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not influenced by potassium acetate
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additional information
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K-type allosteric enzyme
-
additional information
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allosteric enzyme
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additional information
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D-glucose 1,6-bisphosphate and phosphoenolpyruvate have no effect on activity
-
additional information
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not activated by fructose 2,6-bisphosphate
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