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Information on EC 2.7.1.11 - 6-phosphofructokinase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00511

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EC Tree
IUBMB Comments
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
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Oryctolagus cuniculus
UNIPROT: P00511
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phosphofructokinase, 6-phosphofructokinase, 6-phosphofructo-1-kinase, pfk-1, phosphofructokinase-1, pfk-m, phosphofructokinase 1, atp-dependent phosphofructokinase, atp-pfk, pfk-l, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphofructokinase 1
-
1-phosphofructokinase
-
-
6-phosphofructo 1-kinase
-
-
6-phosphofructo-1-kinase
-
-
6-phosphofructokinase, platelet type
-
-
-
-
6-phosphofructose 1-kinase
-
-
-
-
6-phosphofructose-1-kinase
-
-
-
-
ATP-dependent 6-phosphofructokinase
-
-
ATP-dependent phosphofructokinase
-
-
-
-
ATP-PFK
-
-
-
-
ATP: D-fructose-6-phosphate-1-phosphotransferase
-
-
ATP:D-fructose-6-phosphate-1-phosphotransferase
-
-
D-fructose-6-phosphate 1-phosphotransferase
-
-
-
-
fructose 6-phosphate kinase
-
-
-
-
fructose 6-phosphokinase
-
-
-
-
kinase, phosphofructo- (phosphorylating)
-
-
-
-
nucleotide triphosphate-dependent phosphofructokinase
-
-
-
-
PFK1
-
-
-
-
PFK2
-
-
-
-
phospho-1,6-fructokinase
-
-
-
-
phosphofructokinase
-
-
-
-
phosphofructokinase 1
-
-
-
-
phosphofructokinase-1
-
-
phosphohexokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose-6-phosphate 1-phosphotransferase
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-80-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
show the reaction diagram
-
5% of activity with D-fructose 6-phosphate
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
calmodulin binding to the enzyme is stimulated by 0.01 mM Ca2+
Mn2+
-
activation
additional information
-
Na+ has little or no effect at 140 nM PFK-1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aurintricarboxylic acid
-
(-)-Hydroxycitrate
-
-
2,3-diphosphoglycerate
-
-
3-phosphoglycerate
-
1.5-2.0 mM, 50% inhibition
Agaric acid
-
-
Antibodies against rabbit muscle enzyme
-
not rabbit erythrocyte, leukocyte or platelet enzyme
-
Arachidonoyl-CoA
-
-
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
citrate
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
linoleoyl-CoA
-
-
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+
oleoyl-CoA
-
-
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
S-hexadecyl-CoA
-
-
Succinic anhydride
-
muscle and heart enzymes, mechanism
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose 2,6-bisphosphate
-
Aldolase
-
about 120% activity in the presence of 0.005 mM aldolase
-
Calmodulin
D-fructose 2,6-bisphosphate
glutathione
-
activation
Sodium acetate
-
about 115% activity in the presence of 0.04 mM sodium acetate
trehalose
-
activates
additional information
-
not influenced by potassium acetate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kinetic data of various organism
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
ATP
-
pH 7.1
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0039
aurintricarboxylic acid
Oryctolagus cuniculus
pH 8.0, temperature not specified in the publication
0.0015
palmitoyl-CoA
Oryctolagus cuniculus
-
in 50 mM imidazole, pH 8.0, containing 50 mM KCl and 2 mM MgCl2, at 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120 - 160
-
skeletal muscle PFK
139
-
erythrocyte enzyme
50
-
liver PFK
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutations in the muscle 6-phosphofructokinase gene cause Tarui disease
physiological function
-
the enzyme catalyzes the first committed and rate-determining step of glycolysis and thus represents an essential metabolic control point or node for carbohydrate utilization
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PFKAM_RABIT
780
0
85203
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
360000
-
gel filtration at high ionic strength, in 50 mM Tris-phosphate buffer plus 5 mM dithiothreitol, the enzyme aggregates to higher molecular weight form of 520000 Da
380000
-
skeletal muscle
500000
-
erythrocyte, sucrose density gradient centrifugation
67000
-
6 * 67000, muscle enzyme, sedimentation equilibrium ultracentrifugation or gel filtration in 6.5 M guanidine
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
x-ray crystallography
dimer
-
calmodulin-bound dimers are active and less susceptible to inhibition by allosteric ligands, 5 mM ATP stabilizes phosphofructokinase dimers
hexamer
-
6 * 67000, muscle enzyme, sedimentation equilibrium ultracentrifugation or gel filtration in 6.5 M guanidine
tetramer
-
binding of calmodulin to the high affinity site of 6-phosphofructo-1-kinase induces dimerization of the enzyme, but does not inhibit the catalytic activity. Dissociation of the enzyme tetramers induced by calmodulin occurs under very low concentrations of the Ca2+-binding protein and requires Ca2+
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
in vitro phosphorylation of PFK fragment containing a cAMP-dependent protein kinase consensus site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 16% (w/v) PEG 400, 0.1 M MgSO4, and 0.1 M acetate buffer (pH 5.3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R481D
-
no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP, 10% of wild-type PFK activation with 0.1 mM fructose 2,6-bisphosphate
R481L
-
no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP
R48L
-
similar specific activity as wild-type, less sensitive to ATP inhibition, not inhibited by citrate and 3-phosphoglycerate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
complete inactivation after 2 h without stabilizing agent, no inactivation after 2 h incubation in the presence of 1 M trehalose, enzyme incubated in the presence of 37.5% (v/v) glycerol is not protected against incubation at 50°C. Incubation for 45 min at 50°C in the presence of 7.5–25% glycerol (v/v) results in a 2-4times lower activity compared to control
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution inactivates
-
dilution reversibly decreases activity
-
freeze-drying inactivates, addition of Zn2+ plus trehalose, maltose, sucrose, galactose or glucose stabilizes, more than 80% of the initial activity is retained in the presence of 0.4 mM Zn2+ and 100 mM trehalose, no stabilization in the presence of glucose or galactose or any other divalent cation alone
-
fructose 6-phosphate, fructose 1,6-bisphosphate and ammonium sulfate stabilize dilute enzyme solutions
-
glycine, proline, hydroxyproline, trimethylamine N-oxide, glycerol or myo-inositol affords a high degree of cryoprotection
-
very stable in Tris-phosphate or glycylglycine-glycerol buffer, pH 8, at 10-20 mg protein per ml
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, more than 2 mg protein per ml, in 50 mM Tris-phosphate buffer, pH 8, 2 mM EDTA, 100 mM ammonium sulfate, 0.1 mM ATP, 0.5 mM dithiothreitol, several months
-
-20°C, purified enzyme with 10% glycerol (v/v), 2 weeks, no loss of activity
-
4°C, crystalline, 6 years
-
very stable in Tris-phosphate or glycylglycine-glycerol buffer, pH 8, at high protein concentrations
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cibacron Blue 3GA gel filtration, DE-52 column chromatography and ATP-N6-agarose column chromatography
ammonium sulfate precipitation DEAE-Sephacel gel filtration and Bio-Gel filtration
-
liver PFK, ammonium sulfate, DEAE-Sephadex, agarose chromatography
-
liver PFK, heat treatment, protamine sulfate, ammonium sulfate, Sephacryl S-400
-
muscle PFK, isopropanol, heat treatment, ammonium sulfate, crystalization
-
PEG 6000 precipitation, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a pfk-deficient Escherichia coli strain DF1020DE3
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
assay for phosphofructokinase-1 using capillary electrophoresis based on the separation and detection by ultraviolet absorbance at 260 nm of Mg-ATP and Mg-ADP. The separation is enhanced by the addition of Mg2+ to the separation buffer. the assay for directly monitors the enzyme-catalyzed reaction
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kemp, R.G.
Phosphofructokinase from rabbit liver
Methods Enzymol.
42C
67-71
1975
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kemp, R.G.
Phosphofructokinase from yeast
Methods Enzymol.
42C
71-77
1975
Oryctolagus cuniculus
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team