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ATP + D-fructose 6-phosphate
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
-
-
-
?
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
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
-
5% of activity with D-fructose 6-phosphate
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + 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
-
?
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aurintricarboxylic acid
-
2,3-diphosphoglycerate
-
-
3-phosphoglycerate
-
1.5-2.0 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
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
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-phosphate
-
-
K+
-
about 30% residual activity of 30 nM PFK-1 in the presence of 0.2 M K+
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
-
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
Maleic anhydride
-
muscle and heart enzymes, mechanism
Mg2+
-
brain enzyme, at high concentrations
Na+
-
about 70% residual activity of 30 nM PFK-1 in the presence of 0.2 M Na+
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
palmitoylcarnitine-CoA
-
-
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
Succinic anhydride
-
muscle and heart enzymes, mechanism
ATP
-
-
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
citrate
-
-
citrate
-
strong inhibition
citrate
-
50% inhibition below 0.25 mM
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+
additional information
-
photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
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
-
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Bloxham, D.P.; Lardy, H.A.
Phosphofructokinase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
8
239-278
1973
Klebsiella aerogenes, Arthrobacter crystallopoietes, Glutamicibacter nicotianae, Bos taurus, Brassica oleracea var. gemmifera, Saccharomyces cerevisiae, Gallus gallus, Clostridium pasteurianum, Oryctolagus cuniculus, Daucus carota, Dictyostelium discoideum, Escherichia coli, Fasciola hepatica, Thermus thermophilus, Ovis aries, Homo sapiens, Lactiplantibacillus plantarum, Lacticaseibacillus casei, Mus musculus, Neurospora crassa, Pisum sativum, Rattus norvegicus, Zea mays
-
brenda
Starling, J.A.; Allen, B.L.; Kaeini, M.R.; Payne, D.M.; Blytt, H.J.; Hofer, H.W.; Harris, B.G.
Phosphofructokinase from Ascaris suum. Purification and properties
J. Biol. Chem.
257
3795-3800
1982
Ascaris suum, Oryctolagus cuniculus
brenda
Kemp, R.G.
Phosphofructokinase from rabbit liver
Methods Enzymol.
42C
67-71
1975
Oryctolagus cuniculus
brenda
Kemp, R.G.
Phosphofructokinase from yeast
Methods Enzymol.
42C
71-77
1975
Oryctolagus cuniculus
-
brenda
Carpenter, J.F.; Crowe, L.M.; Crowe, J.H.
Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations
Biochim. Biophys. Acta
923
109-115
1987
Oryctolagus cuniculus
brenda
McCune, S.A.; Foe, L.G.; Kemp, R.G.; Jurin, R.R.
Aurintricarboxylic acid is a potent inhibitor of phosphofructokinase
Biochem. J.
259
925-927
1989
Oryctolagus cuniculus
brenda
Massey, T.; Deal, W.C.
Phosphofructokinase from porcine liver and kidney and from other mammalian tissues
Methods Enzymol.
42C
99-110
1975
Bos taurus, Capra hircus, Gallus gallus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Sus scrofa
brenda
Zhao, Z.; Pascalar, R.W.; Malencik, D.A.; Anderson, S.R.
Rabbit liver phosphofructokinase: rapid purification and phosphorylation site identification
Biochem. Biophys. Res. Commun.
222
410-415
1996
Oryctolagus cuniculus
brenda
Li, Y.; Rivera, D.; Ru, W.; Gunasekera, D.; Kemp, R.G.
Identification of allosteric sites in rabbit phosphofructo-1-kinase
Biochemistry
38
16407-16412
1999
Oryctolagus cuniculus
brenda
Zancan, P.; Rosas, A.O.; Marcondes, M.C.; Marinho-Carvalho, M.M.; Sola-Penna, M.
Clotrimazole inhibits and modulates heterologous association of the key glycolytic enzyme 6-phosphofructo-1-kinase
Biochem. Pharmacol.
73
1520-1527
2007
Oryctolagus cuniculus
brenda
Faber-Barata, J.; Sola-Penna, M.
Opposing effects of two osmolytes - trehalose and glycerol--on thermal inactivation of rabbit muscle 6-phosphofructo-1-kinase
Mol. Cell. Biochem.
269
203-207
2005
Oryctolagus cuniculus
brenda
Marinho-Carvalho, M.M.; Zancan, P.; Sola-Penna, M.
Modulation of 6-phosphofructo-1-kinase oligomeric equilibrium by calmodulin: formation of active dimers
Mol. Genet. Metab.
87
253-261
2006
Oryctolagus cuniculus
brenda
Russell, P.; Williams, A.; Marquez, K.; Tahir, Z.; Hosseinian, B.; Lam, K.
Some characteristics of rabbit muscle phosphofructokinase-1 inhibition by ascorbate
J. Enzyme Inhib. Med. Chem.
23
411-417
2008
Oryctolagus cuniculus
brenda
Marinho-Carvalho, M.M.; Costa-Mattos, P.V.; Spitz, G.A.; Zancan, P.; Sola-Penna, M.
Calmodulin upregulates skeletal muscle 6-phosphofructo-1-kinase reversing the inhibitory effects of allosteric modulators
Biochim. Biophys. Acta
1794
1175-1180
2009
Oryctolagus cuniculus
brenda
Russell, P.; Williams, A.; Marquez, K.; Hua, T.; Ehya, F.; Hardamon, C.; Tallman, T.; Valdez, P.
Effect of ammonium, sodium, and potassium ions on rabbit muscle phosphofructokinase-1 and adenylate kinase activities
J. Enzyme Inhib. Med. Chem.
24
930-936
2009
Bos taurus, Oryctolagus cuniculus
brenda
Brueser, A.; Kirchberger, J.; Schoeneberg, T.
Altered allosteric regulation of muscle 6-phosphofructokinase causes Tarui disease
Biochem. Biophys. Res. Commun.
427
133-137
2012
Oryctolagus cuniculus, Homo sapiens
brenda
Jenkins, C.M.; Yang, J.; Sims, H.F.; Gross, R.W.
Reversible high affinity inhibition of phosphofructokinase-1 by acyl-CoA: a mechanism integrating glycolytic flux with lipid metabolism
J. Biol. Chem.
286
11937-11950
2011
Oryctolagus cuniculus
brenda
Russell, P.; Williams, A.; Abbott, A.; Chadwick, J.; Ehya, F.; Flores, R.; Hardamon, C.
Effect of lithium salts on lactate dehydrogenase, adenylate kinase, and 1-phosphofructokinase activities
J. Enzyme Inhib. Med. Chem.
25
551-556
2010
Oryctolagus cuniculus
brenda
Banaszak, K.; Mechin, I.; Obmolova, G.; Oldham, M.; Chang, S.H.; Ruiz, T.; Radermacher, M.; Kopperschlaeger, G.; Rypniewski, W.
The crystal structures of eukaryotic phosphofructokinases from bakers yeast and rabbit skeletal muscle
J. Mol. Biol.
407
284-297
2011
Oryctolagus cuniculus (P00511), Oryctolagus cuniculus, Saccharomyces cerevisiae (P16862), Saccharomyces cerevisiae
brenda
Malina, A.; Bryant, S.K.; Chang, S.H.; Waldrop, G.L.; Gilman, S.D.
Capillary electrophoresis-based assay of phosphofructokinase-1
Anal. Biochem.
447
1-5
2014
Oryctolagus cuniculus (P00511)
brenda