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1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
1-carboxymethyl-ATP + D-fructose 6-phosphate
1-carboxymethyl-ADP + D-fructose 1,6-bisphosphate
90% of activity with with ATP
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
ADP + 2'-deoxyadenosine
AMP + ?
-
-
-
?
ADP + adenosine
AMP + ?
-
-
-
?
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + ribose 5-phosphate
AMP + ?
-
-
-
?
ADP + thymidine
AMP + ?
-
-
-
?
AMP + D-fructose 1,6-bisphosphate
ADP + D-fructose 6-phosphate
-
-
-
r
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + adenosine
ADP + ?
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-tagatose 6-phosphate
ADP + ?
-
poor substrate for isoenzyme PFK2
-
-
?
ATP + fructose
ADP + fructose 1-phosphate
-
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
ATP + glucose 6-phosphate
ADP + glucose 1,6-bisphosphate
-
-
?
ATP + ribose
ADP + ribose 1-phosphate
-
-
?
ATP + ribose 5-phosphate
ADP + ribose 1,5-bisphosphate
-
-
?
ATP + sedoheptulose 7-phosphate
ADP + sedoheptulose 1,7-bisphosphate
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
gamma-thio-ATP + fructose 6-phosphate
ADP + fructose 1-thio-phosphate-6-phosphate
3000fold lower kcat than with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
additional information
?
-
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
-
-
-
?
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
-
-
-
?
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
-
-
-
?
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
-
-
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
for human cells, the measured K0.5(ADP)0:5 values for the reaction with ADP and D-fructose 1,6-bisphosphate exceeds the cytosolic concentrations of ADP, but as steady-state concentrations of F0.5(D-fructose 1,6-bisphosphate) are lower than the K0.5(D-fructose 1,6-bisphosphate) values, it seems likely that under steady-state conditions the reverse reaction would indeed be inefficient. However, cells can be subjected to extreme conditions of stress and nutrient deprivation and the phosphofructokinase reverse flux may be very different in non-steady state, glucose-poor conditions and Q values of 500 or above can easily be achieved if ATP or glucose-6-phosphate are (transiently) depleted
-
-
r
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
key enzyme of glucose metabolism
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
absolutely specific for fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
the enzyme is involved in the ribulose monophosphate cycle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
the enzyme is involved in the ribulose monophosphate cycle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
the enzyme is involved in the ribulose monophosphate cycle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
key regulatory enzyme of glycolysis
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
fructose 6-phosphate shows negative cooperativity at low concentrations and positive cooperativity at high concentrations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with diphosphate as phosphate donor
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
reversible reaction in vivo, but not in vivo, very low activity with acetyl phosphate, UDP and GDP as phosphoryl donors, enzyme is not regulated allosterically
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
Dunaliella marina
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with glucose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
best phosphoryl donors and acceptors of PFK1 and PFK2
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with hexitol 6-phosphates
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
two types of phosphofructokinase-1 (PFK-L and PFK-M) differentially regulate the glycolytic pathway in insulin-stimulated chicken skeletal muscle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
35fold lower reverse reaction velocity
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
key glycolytic enzyme
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
the enzyme catalyzes a rate-limiting reaction in glycolysis
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
the enzyme is involved in glycolysis
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
all three human PFK isoforms can catalyse the reverse reaction in vitro
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no cooperativity with respect to fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
fructose 6-phosphate shows cooperativity
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
50% reduction of PFK expression leads to a proportionally decrease of growth rate, glycolytic flux and lactate flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
sigmoid response to fructose 6-phosphate concentration
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
importance of phosphofructokinase-M for insulin secretion
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
phosphofructokinase-1 is an important control point in the glycolytic pathway, it is implicated in the functions of astrocytes and neurons
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with glucose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
transfers gamma-phosphate of ATP to C-1-hydroxyl of D-(-)fructose 6-phosphate, highly specific for sugar substrate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
glycolytic enzyme
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
the enzyme shows an extremely high degree of cooperative binding, resulting in a virtual on/off switch for substrate concentrations near its K1/2 value
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
important control point for glycolytic flux in the pathway from glucose to fatty acid in the lactating mammary gland, PFK is reactivated by re-feeding of starved animals
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
reducing fructose 6-phosphate concentration results in dissociation and inactivation
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
high cooperativity with respect to fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
dominant rate-controlling enzyme of glucose degradation via Embden-Meyerhof pathway, involved in generation of glycolytic oscillations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
the enzyme shows cooperative binding for fructose-6-phosphate and non-cooperative binding for ATP. Pfk1 undergoes a large conformational change upon Mg-ATP binding
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
sigmoidal kinetics with fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
sigmoidal kinetics with fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
the enzyme shows strictly high specificity for its phosphoryl donor. ADP, AMP, GDP, and PPi could not substitute for ATP
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
the enzyme shows strictly high specificity for its phosphoryl donor. ADP, AMP, GDP, and PPi could not substitute for ATP
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
engineering to increase antibiotic production
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
improved antibiotic production by deletion of PFKA2, involvement of PFKA2 in determining the carbon flux distribution
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
specific for fructose 6-phosphate, very low activity with UTP and CTP
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
reversible reaction in vitro
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
transfers gamma-phosphate of ATP to C-1-hydroxyl of D-(-)fructose 6-phosphate, highly specific for sugar substrate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
negative and positive cooperative kinetics at low fructose 6-phosphate concentrations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
poor substrates are fructose 1-phosphate, glucose 1-phosphate and sedoheptulose 7-phosphate
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
-
-
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
60fold lower kcat than with fructose 6-phosphate
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
-
5% of activity with D-fructose 6-phosphate
-
?
ATP + sedoheptulose 7-phosphate
ADP + sedoheptulose 1,7-bisphosphate
-
-
-
?
ATP + sedoheptulose 7-phosphate
ADP + sedoheptulose 1,7-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
20.6% of the activity with ATP
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
20.6% of the activity with ATP
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
55% of activity with ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
less effective than ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
ITP, GTP or UTP as phosphoryl donors
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
as effective as ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 28% the rate of ATP
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 28% the rate of ATP
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
less effective than ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
13% of activity with ATP
-
?
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
-
-
-
?
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
-
as good as ATP
-
?
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
-
as good as ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
76% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
84.1% of the activity with ATP
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
84.1% of the activity with ATP
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
100% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
less effective than ATP or ITP, better than UTP or CTP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
almost as effective as ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 35% the rate of ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 35% the rate of ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
almost as effective as ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
42% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
64% of activity of ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
76% of activity with ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
130% of activity with ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
less effective than ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
better than GTP, UTP or CTP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 71% the rate of ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 71% the rate of ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
less effective than ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
38% of activity with ATP
-
?
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
?
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
?
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
-
10% of activity with ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
40% of activity with ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
purine NTPs preferred
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
less effective than ATP, ITP, GTP, better than CTP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
as effective as ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 16% the rate of ATP
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
phosphorylation at 16% the rate of ATP
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
14% of activity with ATP
-
?
additional information
?
-
-
the enzyme does also use 2-dehydro-3-deoxy-D-galactonate as substrate
-
-
?
additional information
?
-
the enzyme does also use 2-dehydro-3-deoxy-D-galactonate as substrate
-
-
?
additional information
?
-
-
insulin may increase the glucose consumption in human erythrocytes, through a mechanism involving Ca2+ influx, calmodulin and the detachment of 6-phosphofructose-1-kinase from the erythrocyte membrane
-
-
?
additional information
?
-
-
structure of the ATP-bound state of phosphofructokinase determined by cryo-electron microscopy
-
-
?
additional information
?
-
-
6-phosphofructokinase is the most important element for control of glycolytic flux
-
-
?
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(NH4)2SO4
-
inhibits above 50 mM
1,3-diphosphoglycerate
-
0.385 mM and 0.005 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
2',3'-dialdehyde ATP
-
irreversibly modifies a single lysine residue in the ATP-inhibitory site, thereby locking PFK in a permanantly inhibited state without affecting the integrity of the active site
2,3-diphosphoglycerate
-
-
ammonium sulfate
50 mM, 50% inhibition
Antibodies against rabbit muscle enzyme
-
not rabbit erythrocyte, leukocyte or platelet enzyme
-
ascorbate
-
inhibition by ascorbate is PFK-1 concentration dependent. Ascorbate does not inhibit above 200 nM PFK-1. It is concluded that ascorbate inhibits PFK-1 dimers (and perhaps monomers) but not PFK-1 tetramers
cis-aconitate
-
brain, not heart
clotrimazole
-
clotrimazole alone induces dimerization of the enzyme reducing the population of tetramers, which is not observed when calmodulin is also present. Since PFK dimers are less active than tetramers, this can explain the inhibitory effect of clotrimazole
D-fructose 1,6-bisphosphate
D-fructose 6-phosphate
inhibition occurs at low concentrations of fructose 6-phosphate
D-Glucose 1,6-bisphosphate
D-glucose 6-phosphate
Dunaliella marina
-
weak inhibition
Dithionitrobenzoic acid
-
0.06 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
EDTA
5 mM, complete loss of activity
Li2CO3
-
about 75% residual activity at 20 mM, about 40% residual activity at 40 mM, about 10% residual activity at 100 mM, less than 3% residual activity at 200 mM
Li2SO4
-
about 55% residual activity at 100 mM, about 30% residual activity at 200 mM
lithium acetate
-
about 80% residual activity in the presence of 0.009 mM lithium acetate
MgADP-
addition of MgADP has little effect the specific activity of the enzyme, but diminishes the homotropic cooperativity of fructose 6-phosphate binding, reducing the Hill numbers from 1.6 to 1
p-Chloromercurisulfonic acid
-
0.025 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
palmitoylcarnitine-CoA
-
-
Protein factor
-
19000 Da protein promotes Zn2+ or Fe2+-dependent dissociation into inactive protomers, maximal inactivation at 0.001-0.02 mM Zn2+, inactivation is abolished at higher Zn2+ concentrations, Ca2+, Mg2+, Mn2+ can substitute for Zn2+ or Fe2+ only at millimolar concentrations, potency in descending order: Mn2+, Mg2+, Ca2+, inactivation can be reversed by the addition of ATP, fructose 1,6-bisphosphate, or fructose 2,6-bisphosphate
-
2-oxoglutarate
-
competitive inhibition
2-oxoglutarate
-
2 mM, 92% inhibition
2-oxoglutarate
-
brain PFK, not heart PFK
2-phosphoglycerate
-
2 mM and 3.2 mM, 50% inhibition of cytosolic PFK at pH 8.0 and PH 7.2, respectively, 0.5 mM and 0.4 mM, 50% inhibition of plastid PFK at pH 8.0 and pH 7.2, respectively
2-phosphoglycerate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, kinetics
2-phosphoglycerate
-
0.032 mM and 0.004 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
2-phosphoglycerate
-
1.3 mM, 50% inhibition of cytosolic PFK, no inhibition in the presence of 5 or 25 mM phosphate
3-phosphoglycerate
-
-
3-phosphoglycerate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, 0.5 mM, 50% inhibition, sigmoidal inhibition curve; inhibition kinetics
3-phosphoglycerate
-
2 mM, 86% inhibition; inhibition kinetics
3-phosphoglycerate
-
1.5-2.0 mM, 50% inhibition
3-phosphoglycerate
-
0.9 mM, 50% inhibition of plastid PFK
3-phosphoglycerate
-
mixed inhibition
3-phosphoglycerate
-
about 70% inhibition at 7 mM
ADP
1 mM, 82% inhibition
ADP
-
most potent inhibitor of cytosolic isozyme, 0.4 mM and 4 mM, 50% inhibition of cytosolic and plastid PFK at pH 8.0
ADP
Dunaliella marina
-
-
ADP
-
complete inhibition at 4.5 mM ADP, 52.4% residual activity at 2.3 mM ADP
ADP
substrate inhibition above 2 mM; substrate inhibition above 2 mM; substrate inhibition above 2 mM
ADP
-
1.9 mM and 0.0006 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
Aldolase
-
-
-
AMP
1 mM and 4 mM, 20% and 40% inhibition in the presence of 5 mM fructose 6-phosphate and Mg2+
AMP
-
at high fructose 6-phosphate concentrations, activates at low fructose 6-phosphate concentrations
AMP
-
5 mM, 80% inhibition
ATP
-
-
ATP
-
fructose 6-phosphate partially reverses inhibition
ATP
-
above 0.05 mM, inhibition is more pronounced at pH 6.6 but occurs also at pH 8.0, inhibition is reversed by equivalent amounts of AMP
ATP
-
synergistic with citrate
ATP
in contrast to the native PFK1 enzyme, the 49 kDa PFK1 fragment is highly sensitive to ATP inhibition (5fold lower activity at the 1 mM ATP than at the 0.1 mM concentration)
ATP
-
at high concentrations
ATP
nearly complete inhibition at 5 mM ATP
ATP
-
inhibition above 0.08 mM
ATP
-
cytosolic isoenzyme is more sensitive to inhibition at pH 8.0 than pH 7.2, Mg2+ alleviates inhibition
ATP
-
at high concentrations
ATP
-
2 mM, 50% inhibition of cytosolic PFK at pH 8.0, 5 mM, 50% inhibition of plastid PFK at pH 8.0
ATP
Dunaliella marina
-
strong inhibition above 1 mM, at 2.5 mM Mg2+
ATP
-
at alkaline pH; mechanism
ATP
inhibition of fructose 1-phosphate phosphorylation above 0.08 mM ATP
ATP
-
1 mM, almost complete inhibition of native PFK, phosphorylated PFK is less sensitive to inhibition
ATP
-
inhibition of M-type PFK above 0.1 mM
ATP
-
millimolar inhibitor
ATP
-
ADP partially reverses inhibition
ATP
-
above 1 mM at 0.33 mM fructose 6-phosphate and 2 mM Mg2+, inhibition at a Mg/ATP ratio below 2; ADP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; Mg2+ partially reverses inhibition
ATP
-
in the absence of AMP and fructose 2,6-bisphosphate
ATP
-
fructose 2,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
at high concentrations
ATP
-
above 0.2 mM, inhibition is alleviated by Mg2+; free form
ATP
-
ADP partially reverses inhibition; cAMP partially reverses inhibition; fructose 1,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
ADP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
above 0.25 mM in the absence of MgCl2; free form
ATP
-
0.99 mM, 50% inhibition
ATP
-
0.02 mM and 0.94 mM, 50% inhibition at 0.0001 mg/ml and at 0.0006 mg/ml PFK respectively, 3.23 mM, 50% inhibition at 0.0006 mg/ml PFK in the presence of 10% polyethylene glycol
ATP
-
muscle PFK, strong inhibition at pH 7.1, weak inhibition at pH 7.6-8.5, not inhibited at pH 9.0
ATP
-
0.4 mM, 50% inhibition of PFK C
ATP
-
the inhibition of enzyme activity by ATP (above 1 mM) is abolished in the presence of calmodulin
ATP
-
cAMP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; pH-dependent inhibition; phosphate and AMP partially reverse inhibition
ATP
-
7.5 mM, 98% inhibition; fructose 2,6-bisphosphate partially reverses inhibition
ATP
-
fructose 1,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
pH-dependent inhibition
ATP
-
inhibition of plastid PFK above 5 mM at pH 8.0 and above 0.5 mM at pH 7.2
ATP
-
substrate inhibition
ATP
-
NaF and limited proteolysis protect from inhibition
ATP
-
lower inhibition at pH 6.6 compared to pH 7.2
ATP
-
above 1 mM, inhibition is relieved by Mg2+; free form
ATP
-
potentiates inhibitory action of citrate
ATP
-
complete inhibition at 10 mM
ATP
-
1 mM, 90% inhibition of the activity observed with 0.1 mM ATP
ATP
-
at physiological concentration; at physiological pH, the enzyme is allosterically inhibited by near-physiological concentrations of its co-substrate ATP, which induces cooperativity, i.e. reduces the affinity for the substrate fructose 6-phosphate. Inhibition by ATP is reinforced by citrate and H+
ATP
-
allosteric inhibition by high ATP concentrations. The inhibitory effects of high ATP concentration can be reversed by D-fructose 2,6-bisphosphate and AMP
ATP
-
0.004 mM and 0.003 mM, 50% inhibition at 20°C and 6°C, respectively, normoxic turtles
aurintricarboxylic acid
-
0.0002 mM, 50% inhibition at pH 7.3, reversed by addition of allosteric activators, i.e., fructose 2,6-bisphosphate or AMP, no inhibition at pH 8.0
aurintricarboxylic acid
-
Ca2+
-
competitive vs. Mg2+
Ca2+
-
depending upon total Mg2+-concentration, kinetics, cytosolic isozyme
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition
citrate
-
weak inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition; synergistic with ATP; synergistic with NH4+; synergistic with phosphate and AMP
citrate
the native 85000 Da enzyme is moderately inhibited by citrate, the 49000 Da shorter fragment of PFK1 proves to be completely resistant to inhibition by citrate
citrate
when 5 mM of citrate is added a moderate reduction for about 1020% is recorded in the homogenate of TE22 and TE23 strain, while in A158 strain much stronger reduction of PFK1 specific activity, for approximately 40% is observed
citrate
-
strong inhibition
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
presence of 12 mM Mg2+ relieves inhibition completely
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition
citrate
-
strong inhibition
citrate
Dunaliella marina
-
-
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition
citrate
-
strong inhibition; weak inhibition
citrate
-
strong inhibition
citrate
-
strong inhibition
citrate
-
strong inhibition
citrate
-
weak inhibition
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
weak inhibition
citrate
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
citrate
-
2 mM, complete inhibition
citrate
-
strong inhibition
citrate
-
10 mM, 60% inhibition
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
0.12 mM, 50% inhibition
citrate
-
strong inhibition
citrate
-
50% inhibition below 0.25 mM
citrate
-
strong inhibition
citrate
-
strong inhibition; weak inhibition
citrate
-
strong inhibition
citrate
-
with glucose 1,6-bisphosphate or fructose 1,6-bisphosphate as activator
citrate
-
strong inhibition; synergistic with phosphate and AMP
citrate
-
at pH 7.6, not at pH 8.4
citrate
-
inhibition of M- and C-type PFK in pancreatic beta-cells
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
almost complete inhibition at 1 mM citrate in the absence of D-fructose 2,6-bisphosphate
citrate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
citrate
-
strong inhibition
citrate
-
0.23 and 0.17 mM mM, 50% inhibition at 20° and 6°C, respectively, normoxic turtles, 0.3 mM, 50% inhibition at 20°C and 6°C, anoxic turtles
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
10 mM, approx. 30% inhibition
citrate
-
strong inhibition
CTP
-
-
CTP
-
free form, Mg2+ relieves
Cu2+
1 mM, 52.4% inhibition
Cu2+
-
0.001 mM, 28% inhibition
D-fructose 1,6-bisphosphate
-
0.02 mM, 50% inhibition in the presence of physiological concentrations of ATP, AMP, phosphate and fructose 6-phosphate
D-fructose 1,6-bisphosphate
-
0.02 mM, 50% inhibition at 100 mM fructose 6-phosphate in the absence of fructose 2,6-bisphosphate, inhibition is reversed by fructose 2,6-bisphosphate
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
5 mM, 25% inhibition
D-fructose 1,6-bisphosphate
-
in the absence of fructose 2,6-bisphosphate
D-fructose 1,6-bisphosphate
-
product inhibition
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Fructose 1-phosphate
-
-
D-Glucose 1,6-bisphosphate
-
0.08 mM, 50% inhibition in the presence of physiological concentrations of ATP, AMP, phosphate and fructose 6-phosphate, inhibition is relieved by 50% by 0.008 mM fructose 2,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
in the absence of fructose 2,6-bisphosphate
diphosphate
1 mM, 21% inhibition
diphosphate
1 mM and 4 mM, 20% and 50% inhibition in the presence of 5 mM fructose 6-phosphate and 5 mM Mg2+
diphosphate
-
inactivates under assay conditions
diphosphate
-
0.1 mM, 80% inhibition, nucleotide diphosphates, i.e. ADP, GDP or TDP, partially alleviate inhibition
GDP
1 mM, 46% inhibition
GDP
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
GTP
-
plastid, not cytosolic, isozyme
GTP
-
free form, Mg2+ relieves
isocitrate
-
competitive inhibition
isocitrate
-
brain, not heart
isocitrate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
K+
-
about 30% residual activity of 30 nM PFK-1 in the presence of 0.2 M K+
K+
-
at high concentrations, ATP reverses
K+
-
about 30% residual activity of 30 nM PFK-1 in the presence of 0.2 M K+
KCl
100 mM, 50% inhibition
KCl
-
inhibits above 50 mM
Lactate dehydrogenase
-
lactate dehydrogenase suspended in 3.2 M ammonium sulfate inhibits 30 nM PFK-1 resulting in a more than 50% inhibition of activity
-
Lactate dehydrogenase
-
lactate dehydrogenase suspended in 3.2 M ammonium sulfate inhibits 30 nM PFK-1 resulting in a more than 50% inhibition of activity
-
malate
-
competitive inhibition
malate
-
2 mM, 92% inhibition
malate
-
kidney cortex, brain, not heart
malate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
Maleic anhydride
-
muscle and heart enzymes, mechanism
Maleic anhydride
-
muscle and heart enzymes, mechanism
Maleic anhydride
-
muscle and heart enzymes, mechanism
Mg2+
-
brain enzyme, at high concentrations
Mg2+
-
brain enzyme, at high concentrations
Mg2+
-
brain enzyme, at high concentrations
Mg2+
-
free form, citrate reverses, independent of MgATP-concentration, kinetics, cytosolic isozyme
MgATP2-
-
cytosolic isozyme
MgATP2-
inhibition occurs at high concentrations of MgATP2-
Na+
-
about 70% residual activity of 30 nM PFK-1 in the presence of 0.2 M Na+
Na+
-
about 70% residual activity of 30 nM PFK-1 in the presence of 0.2 M Na+
NaCl
1 M, 50% inhibition
NH4+
-
about 40% residual activity of 30 nM PFK-1 in the presence of 0.2 M NH4+
NH4+
-
muscle PFK, weak, at high concentrations, activation at very low concentrations
NH4+
-
about 40% residual activity of 30 nM PFK-1 in the presence of 0.2 M NH4+
nucleoside triphosphate
-
-
nucleoside triphosphate
-
at a Mg/NTP ratio below 2
nucleoside triphosphate
-
free form, pH-dependent
palmitoyl-CoA
-
low micromolar inhibitor, MgAMP and MgADP but not MgATP protect the enzyme against inhibition by palmitoyl-CoA. Acyl-protein thioesterase-1 reverses palmitoyl-CoA-mediated enzyme inhibition
phosphatase
-
dephosphorylation inactivates
-
phosphatase
-
dephosphorylation inactivates
-
phosphate
-
inhibition at 10-100 mM, concentrations at 1- 5 mM relieve the influence of other inhibitors such as phosphoenolpyruvate
phosphate
Dunaliella marina
-
above 5 mM; kinetics; the enzyme is both activated and inhibited by phosphate, depending on fructose 6-phosphate/phosphate-ratio
phosphate
-
10 mM, 50% inhibition
phosphate
-
25 mM, 50% and 57% inhibition of PFK-1 at pH 6.6 and pH 7.2, respectively
phosphate
slight inhibition; slight inhibition; slight inhibition
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
0.1 mM, 50% inhibition at low pH; phosphate relieves
phosphoenolpyruvate
-
effective inhibition at 0.005-0.02 mM, fructose 6-phosphate relieves inhibition; most potent inhibitor
phosphoenolpyruvate
-
most potent inhibitor
phosphoenolpyruvate
-
0.04 mM and 0.05 mM, 50% inhibition of plastid PFK at pH 8.0 and pH 7.2, respectively; most potent inhibitor
phosphoenolpyruvate
Dunaliella marina
-
1 mM, complete inhibition, 0.08 mM, 50% inhibition; inhibition kinetic; phosphate relieves
phosphoenolpyruvate
-
feedback inhibition
phosphoenolpyruvate
I153V mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
phosphoenolpyruvate
-
5 mM; 64% inhibition
phosphoenolpyruvate
-
2 mM, complete inhibition; inhibition kinetic
phosphoenolpyruvate
-
inhibition of mammary gland PFK
phosphoenolpyruvate
-
0.0023 mM and 0.0009 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
phosphoenolpyruvate
-
0.59 mM, 50% inhibition
phosphoenolpyruvate
-
at pH 7.6, not at pH 8.4
phosphoenolpyruvate
-
0.05 mM, 50% inhibition of plastid PFK
phosphoenolpyruvate
-
mixed inhibition
phosphoenolpyruvate
-
about 30% inhibition at 5 mM
phosphoenolpyruvate
-
0.22 mM, 50% inhibition of cytosolic PFK in the presence of 1 mM fructose 6-phosphate, phosphate relives inhibition
phosphoenolpyruvate
-
0.1 mM and 10 mM, allosteric inhibition, almost completely reversed by 2.5 mM ADP
phosphoenolpyruvate
addition leads to a decease in fructose 6-phosphate binding affinity and in heterotropically induced homotropic cooperativity in fructose 6-phosphate binding, the Hill numbers increase from 1.6 to above 2.5 without decrease in specific activity
phosphoenolpyruvate
-
inhibition kinetic
phosphoenolpyruvate
-
1 mM, approx. 75% inhibition
Phosphoglycolate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, kinetics
Phosphoglycolate
-
0.006 mM and 0.003 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
Phosphoglycolate
-
0.25 mM, 50% inhibition of plastid PFK
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
SO42-
-
-
SO42-
-
20 mM, 50% inhibition of cytosolic and 77% inhibition of plastid PFK at pH 7.2, not at pH 8.0
SO42-
-
2 mM, 50% inhibition at pH 7.2, 5 mM complete inhibition
succinate
-
competitive inhibition
succinate
-
kidney cortex and brain PFK, heart PFk is not inhibited
Succinic anhydride
-
muscle and heart enzymes, mechanism
Succinic anhydride
-
muscle and heart enzymes, mechanism
Succinic anhydride
-
muscle and heart enzymes, mechanism
UTP
does not inhibit activity to the same extent as ATP
UTP
-
free form, Mg2+ relieves
Zn2+
-
-
Zn2+
-
0.001 mM, 28% inhibition
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by cAMP
-
additional information
the active 49 kDa PFK1 fragment is not inhibited by citrate
-
additional information
-
the active 49 kDa PFK1 fragment is not inhibited by citrate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP
-
additional information
-
not inhibited by ADP; not inhibited by Ca2+; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
cytosolic PFK is not inhibited by GTP; not inhibited by fructose 2,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP
-
additional information
Dunaliella marina
-
not inhibited by ADPglucose, dithiothreitol, gluconate 6-phosphate, glucose 1-phosphate; not inhibited by NH4+ and K+
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by pyruvate; not inhibited by ribulose 5-phosphate
-
additional information
no substrate inhibition with gamma-thio-ATP
-
additional information
-
no substrate inhibition with gamma-thio-ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
product inhibition of reverse reaction
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
high insulin concentration decreases enzyme activity in intact cells
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ADP
-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by 3-phosphoglycerate; not inhibited by ADP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by 3-phosphoglycerate; not inhibited by ADP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by fructose 2,6-bisphosphate; not inhibited by glutamine, glutamate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by AMP; not inhibited by cAMP; not inhibited by phosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by AMP; not inhibited by cAMP; not inhibited by phosphate; not inhibited by pyruvate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
acetyl-CoA, malonyl-CoA, palmitoylcarnitine, and palmitic acid in the presence of CoASH are without effect on enzyme activity
-
additional information
-
not inhibited by LiCl
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
heart enzyme, not inhibited by cis-aconitate, L-isocitrate, alpha-ketoglutarate, succinate, fumarate, malate, tricarnallylic acid, CoASH, or acetyl-CoASH; not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by fructose 6-phosphate
-
additional information
-
not inhibited by phosphate
-
additional information
-
cytosolic PFK is not inhibited by ATP and SO42-
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by GTP; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
not inhibited by MgATP2-
-
additional information
-
not inhibited by 6-phosphogluconate and phosphocreatine
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by fructose 2,6-bisphosphate; not inhibited by Na+
-
additional information
-
not inhibited by cAMP; not inhibited by UDP, UDPglucose
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by 3-phosphoglycerate; not inhibited by ADP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by AMP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
effect of low temperature or anoxia on inhibition kinetics
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by fructose 2,6-bisphosphate; not inhibited by phosphate
-
additional information
-
not inhibited by MgATP2-
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
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8.8
2-dehydro-3-deoxy-D-gluconate
at pH 8.0 and 42°C
1.57
AMP
pH 7.5, 50°C, 5 mM Mg2+
0.7 - 16.7
D-fructose 1,6-bisphosphate
0.007 - 254
D-fructose 6-phosphate
90
D-glucose
pH 7.5, 50°C, 5 mM Mg2+
0.6
D-glucose 6-phosphate
pH 6.7, 85°C
3
D-ribose 5-phosphate
pH 6.7, 85°C
0.01 - 0.2
fructose 6-phosphate
2.5
sedoheptulose 7-phosphate
pH 7.0, 55°C
additional information
ADP
0.32
ADP
pH 7.5, 90°C, 5 mM Co2+
0.74
ADP
pH 7.5, 50°C, 5 mM Mg2+
0.86
ADP
pH 7.5, 50°C, 5 mM Co2+
0.005
ATP
-
pH 7.2, 25°C, cytosolic PFK
0.006
ATP
-
pH 7.2, 25°C, plastid PFK
0.007
ATP
-
pH 8.0, 25°C, cytosolic PFK
0.008
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.0087
ATP
-
pH 7.0, 25°C, cytosolic PFK
0.009
ATP
-
pH 7.25, 25°C
0.012
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.013
ATP
-
pH 7.0, 25°C, chloroplasr PFK
0.013
ATP
-
pH 6.7, 37°C, at 0.25 mM fructose 6-phosphate
0.014
ATP
-
pH 8.0, 25°C, plastid PFK
0.0151
ATP
-
mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.017
ATP
-
pH 6.7, 37°C, at 0.4 mM fructose 6-phosphate
0.017
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
0.02
ATP
pH 7.2, 30°C, cosubstrate fructose 1-phosphate
0.02
ATP
pH 7.2, 25°C, red blood cell lysate from diabetic subjects as source of enzyme
0.021
ATP
-
pH 7.3, 25°C, PFK II
0.023
ATP
-
pH 6.7, 37°C, at 0.75 mM fructose 6-phosphate
0.023
ATP
-
pH 7.0, 6°C, normoxic animals
0.0232
ATP
-
mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.026
ATP
-
pH 6.7, 37°C, at 2.0 mM fructose 6-phosphate
0.027
ATP
pH 6.5, 95°C, discontinuous assay
0.0275
ATP
-
mutant enzyme S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.028
ATP
-
pH 8.0, 25°C, cytosolic PFK
0.029
ATP
N-terminal truncation mutant, pH 7.1, 25°C
0.03
ATP
-
pH 7.0, 6°C, anoxic animals
0.0326
ATP
-
mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0338
ATP
-
mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.034
ATP
-
pH 7.0, 20°C, normoxic and anoxic animals
0.034
ATP
-
pH 8.0, 25°C, PFK I
0.0356
ATP
-
mutant enzyme K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0356
ATP
-
mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.037
ATP
wild-type, pH 7.1, 25°C
0.037
ATP
-
mutant enzyme S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0382
ATP
-
mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0384
ATP
-
mutant enzyme K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0415
ATP
-
mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0425
ATP
-
mutant enzyme R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0425
ATP
-
wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.043
ATP
-
mutant enzyme S377A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0432
ATP
-
mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0477
ATP
-
mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.049
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.0498
ATP
-
wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.05
ATP
-
pH 8.2, 28°C, PFK2
0.05
ATP
pH 7.2, 25°C, red blood cell lysate from diabetic subjects as source of enzyme
0.0508
ATP
-
mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.051
ATP
-
purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate
0.0524
ATP
-
mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0528
ATP
-
mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.055
ATP
-
pH 8.5, 30°C, wild-type PFK
0.055
ATP
-
pH 8.5, 30°C, I126A mutant PFK
0.06
ATP
Dunaliella marina
-
pH 7.0
0.063
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0647
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0674
ATP
-
mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0674
ATP
-
mutant enzyme D543A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.07
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
0.076
ATP
-
purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate
0.076
ATP
N-terminal truncation mutant, presence of 5 mM AMP, pH 7.1, 25°C
0.0769
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0894
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 2'-iodo-ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.094
ATP
-
pH 8.5, 30°C, R72H mutant PFK
0.1
ATP
-
12 h after isoproterenol administration, PFK-1
0.11
ATP
-
pH 8.5, 30°C, wild-type PFK
0.114
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.114
ATP
-
mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.117
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.12
ATP
-
pH 8.2, 30°C, native PFK
0.12
ATP
-
pH 8.0, 25°C, erythrocyte PFK
0.13
ATP
-
pH 8.2, 30°C, G212V mutant PFK
0.141
ATP
-
mutant enzyme S377A/K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.151
ATP
-
mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.16
ATP
wild-type, presence of 5 mM AMP, pH 7.1, 25°C
0.166
ATP
-
mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.168
ATP
-
mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.168
ATP
-
mutant enzyme S377A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.169
ATP
-
mutant enzyme D543A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.169
ATP
-
wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.18
ATP
-
ATP in form of MgATP2-
0.2
ATP
-
pH 7.0, 50°C and 75°C
0.22
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.23 - 0.28
ATP
-
pH 7.0, 25°, 37°C and 50°C
0.234
ATP
-
mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.25
ATP
-
mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.3
ATP
at pH 8.0 and 42°C
0.38
ATP
strain PB1, Pfk2, pH 9.0, 30°C
0.39
ATP
strain MGA3, Pfk2, pH 9.0, 30°C
0.6 - 0.9
ATP
pH 7.5, 37°C
0.82
ATP
strain MGA3, Pfk1, pH 9.0, 30°C
0.018
CTP
-
pH 8.0, 25°C, cytosolic PFK
0.019
CTP
-
pH 7.2, 25°C, plastid PFK
0.021
CTP
-
pH 7.2, 25°C, cytosolic PFK
0.03
CTP
-
pH 7.3, 25°C, PFK II
0.033
CTP
-
pH 8.0, 25°C, plastid PFK
0.099
CTP
-
pH 8.0, 25°C, PFK I
0.7
D-fructose 1,6-bisphosphate
pH 7.5, 50°C, 5 mM Mg2+
7.6
D-fructose 1,6-bisphosphate
-
pH 7.0, 75°C
16.7
D-fructose 1,6-bisphosphate
-
pH 6.0, 85°C
0.007
D-fructose 6-phosphate
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.007
D-fructose 6-phosphate
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.011
D-fructose 6-phosphate
-
pH 8.2, 28°C, PFK2
0.018
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.019
D-fructose 6-phosphate
-
-
0.023
D-fructose 6-phosphate
-
pH 7.0 and pH 8.0
0.023
D-fructose 6-phosphate
-
pH 8.2, 30°C, native PFK
0.024
D-fructose 6-phosphate
-
-
0.026
D-fructose 6-phosphate
-
pH 8.2, 30°C, G212V mutant PFK
0.028
D-fructose 6-phosphate
-
pH 8.2, 30°C, cosubstrate GTP
0.03
D-fructose 6-phosphate
-
pH 8.2, 30°C, at fructose 6-phosphate concentrations that are less than approx. one-third the fixed MgATP concentration
0.037
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.043
D-fructose 6-phosphate
-
pH 7.0, 6°C, normoxic animals
0.047
D-fructose 6-phosphate
-
pH 7.1, 25°C, M-type PFK
0.05
D-fructose 6-phosphate
-
-
0.05
D-fructose 6-phosphate
-
pH 6.8, 30°C
0.065
D-fructose 6-phosphate
pH 7.0, 55°C
0.068
D-fructose 6-phosphate
-
pH 8.2, 30°C, cosubstrate UTP
0.071
D-fructose 6-phosphate
-
-
0.086
D-fructose 6-phosphate
-
-
0.095
D-fructose 6-phosphate
-
pH 7.0, 6°C, anoxic animals
0.096
D-fructose 6-phosphate
pH 7.2, 30°C, cosubstrate gamma-thio-ATP
0.106
D-fructose 6-phosphate
-
pH 7.0, 20°C, anoxic animals
0.11
D-fructose 6-phosphate
-
pH 7.0, 20°C, normoxic animals
0.14
D-fructose 6-phosphate
-
pH 8.5, 30°C, D127/R252Q double mutant PFK
0.15
D-fructose 6-phosphate
-
pH 8.2, 30°C, cosubstrate CTP
0.16
D-fructose 6-phosphate
-
pH 8.5, 30°C
0.18
D-fructose 6-phosphate
-
pH 8.4
0.19 - 0.2
D-fructose 6-phosphate
-
-
0.19 - 0.2
D-fructose 6-phosphate
-
-
0.2
D-fructose 6-phosphate
-
pH 8.5, 30°C, D127S mutant PFK
0.24
D-fructose 6-phosphate
-
-
0.25
D-fructose 6-phosphate
-
pH 7.5
0.29
D-fructose 6-phosphate
-
pH 7.15, 25°C, in the presence of 0.1 mM fructose 2,6-bisphosphate
0.29
D-fructose 6-phosphate
pH 7.2, 25°C, red blood cell lysate as source of enzyme
0.3
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 2/1
0.37
D-fructose 6-phosphate
-
pH 7.15, 25°C, in the presence of 1 mM AMP
0.37
D-fructose 6-phosphate
pH 7.2, 25°C, red blood cell lysate as source of enzyme
0.44
D-fructose 6-phosphate
-
pH 7.8, 50°C
0.45
D-fructose 6-phosphate
-
pH 8.0, 25°C, erythrocyte PFK
0.48
D-fructose 6-phosphate
-
pH 8.5, 30°C
0.5
D-fructose 6-phosphate
-
pH 7.9, 24°C
0.55
D-fructose 6-phosphate
pH 7.5, 50°C, 5 mM Mg2+
0.57
D-fructose 6-phosphate
-
pH 6.0, 50°C
0.58
D-fructose 6-phosphate
pH 7.5, 50°C, 5 mM Co2+
0.6
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 1.4/1
0.61
D-fructose 6-phosphate
strain MGA3, Pfk2, pH 9.0, 30°C
0.62
D-fructose 6-phosphate
-
pH 8.0, 25°C
0.68
D-fructose 6-phosphate
pH 6.7, 85°C
0.688
D-fructose 6-phosphate
-
pH 7.0, 55°C
0.71
D-fructose 6-phosphate
-
-
0.74
D-fructose 6-phosphate
pH 7.5, 90°C, 5 mM Co2+
0.79
D-fructose 6-phosphate
strain PB1, Pfk2, pH 9.0, 30°C
0.94
D-fructose 6-phosphate
strain MGA3, Pfk1, pH 9.0, 30°C
1.17
D-fructose 6-phosphate
-
pH 6.0, 85°C
1.212
D-fructose 6-phosphate
pH 6.5, 95°C, discontinuous assay
1.4
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 0.7/1
1.43
D-fructose 6-phosphate
-
pH 7.9
1.44
D-fructose 6-phosphate
-
pH 7.0, 25°C
1.5
D-fructose 6-phosphate
-
-
1.58
D-fructose 6-phosphate
-
pH 7.15, 25°C
1.7
D-fructose 6-phosphate
30°C, pH 7.8
1.8
D-fructose 6-phosphate
-
pH 8.0, phosphorylated PFK
2.15
D-fructose 6-phosphate
-
pH 7.0, 37°C
3.44
D-fructose 6-phosphate
-
pH 7.0, 50°C
7
D-fructose 6-phosphate
-
pH 8.0, native PFK
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
254
D-fructose 6-phosphate
-
pH 8.5, 30°C, R252Q mutant PFK
0.01
fructose 6-phosphate
-
12 h after isoproterenol administration
0.016
fructose 6-phosphate
-
pH 7.0, 25°C, cytosolic PFK
0.039
fructose 6-phosphate
-
pH 8.0, 30°C
0.2
fructose 6-phosphate
-
pH 7.7
0.0006
GTP
-
pH 7.2, 25°C, cytosolic PFK
0.0009
GTP
-
pH 8.0, 25°C, cytosolic PFK
0.008
GTP
-
pH 7.2, 25°C, plastid PFK
0.013
GTP
-
pH 8.0, 25°C, plastid PFK
0.038
GTP
-
pH 7.3, 25°C, PFK II
0.003
ITP
-
pH 8.0, 25°C, pH 7.2, 25°C, cytosolic PFK
0.004
ITP
-
pH 7.2, 25°C, plastid PFK
0.011
ITP
-
pH 8.0, 25°C, plastid PFK
0.035
ITP
-
pH 7.3, 25°C, PFK II
0.082
ITP
-
pH 8.0, 25°C, PFK I
0.01
Mg2+
-
pH 7.9, 24°C
0.009
UTP
-
pH 7.2, 25°C, cytosolic PFK
0.01
UTP
-
pH 8.0, 25°C, plastid PFK
0.018
UTP
-
pH 8.0, 25°C, cytosolic PFK
0.019
UTP
-
pH 7.2, 25°C, plastid PFK
0.032
UTP
-
pH 7.3, 25°C, PFK II
0.055
UTP
-
pH 8.0, 25°C, PFK I
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
ADP
K0.5: 1.382 mM, pH 7.4, 25°C
additional information
ADP
K0.5: 1.768 mM, pH 7.4, 25°C
additional information
ADP
K0.5: 3.137 mM, pH 7.4, 25°C
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 1.287 mM, pH 7.4, 25°C
additional information
D-fructose 1,6-bisphosphate
K0.5: 1.54, pH 7.4, 25°C
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.495 mM, pH 7.4, 25°C
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
Dunaliella marina
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic properties of dansylated enzyme
-
additional information
additional information
-
oligomeric form exhibits negative cooperativity with fructose 6-phosphate
-
additional information
additional information
-
cooperativity with respect to fructose 6-phosphate
-
additional information
additional information
-
effects of low temperature and anoxia on kinetic constants
-
additional information
additional information
-
effects of temperature on kinetic properties
-
additional information
additional information
-
allosteric kinetics at alkaline pH-values
-
additional information
additional information
-
kinetic properties of phosphorylated enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated enzyme
-
additional information
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
additional information
-
kinetic model of phosphofructokinase-1
-
additional information
additional information
allosteric regulation. At saturating fructose 6-phoshate (5 mM), the Hill number for MgATP binding is 0.8
-
additional information
additional information
-
allosteric regulation. At saturating fructose 6-phoshate (5 mM), the Hill number for MgATP binding is 0.8
-
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