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Information on EC 2.7.1.11 - 6-phosphofructokinase and Organism(s) Rattus norvegicus

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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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Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
6-phosphofructokinase, platelet type
-
-
-
-
6-phosphofructose 1-kinase
-
-
-
-
6-phosphofructose-1-kinase
-
-
-
-
ATP-dependent phosphofructokinase
-
-
-
-
ATP-PFK
-
-
-
-
D-fructose-6-phosphate 1-phosphotransferase
-
-
-
-
fructose 6-phosphate kinase
-
-
-
-
fructose 6-phosphokinase
-
-
-
-
kinase, phosphofructo- (phosphorylating)
-
-
-
-
nucleotide triphosphate-dependent phosphofructokinase
-
-
-
-
PFK
-
-
-
-
PFK2
-
-
-
-
phospho-1,6-fructokinase
-
-
-
-
phosphofructokinase
-
-
-
-
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
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
brain PFK, not heart PFK
cis-aconitate
-
brain, not heart
citrate
D-Fructose 1-phosphate
-
-
isocitrate
-
brain, not heart
malate
-
kidney cortex, brain, not heart
Maleic anhydride
-
muscle and heart enzymes, mechanism
Mg2+
-
brain enzyme, at high concentrations
phosphoenolpyruvate
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
-
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
succinate
-
kidney cortex and brain PFK, heart PFk is not inhibited
Succinic anhydride
-
muscle and heart enzymes, mechanism
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose 1,6-bisphosphate
-
activation of PFK in INS-1 cell extract
D-fructose 2,6-bisphosphate
NH4+
-
activation of muscle enzyme, inhibitory at high concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.1
ATP
0.086 - 0.18
D-fructose 6-phosphate
0.01
fructose 6-phosphate
-
12 h after isoproterenol administration
additional information
additional information
-
kinetic data of various organism
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
alpha-ketoglutarate
-
brain PFK
0.1
cis-aconitate
-
brain PFK
0.03
citrate
-
brain PFK
0.2
isocitrate
-
brain PFK
0.6
malate
-
brain PFK
1.5
succinate
-
brain PFK
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175 - 177
-
-
206
-
liver PFK
265
-
muscle PFK
additional information
-
slight increase in rats 12 h after isoproterenol administration
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
small intestine PFK, 85-90% of maximal activity at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27 - 28
-
assay at
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
only M-type, i.e. muscle-type PFK isoenzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
phosphofructokinase1 (PFK1) is the major regulatory enzyme of the glycolytic pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PFKAP_RAT
788
0
85720
Swiss-Prot
other Location (Reliability: 1)
PFKAL_RAT
780
0
85339
Swiss-Prot
other Location (Reliability: 2)
PFKAM_RAT
780
0
85560
Swiss-Prot
other Location (Reliability: 1)
A0A8I6ADR0_RAT
847
0
92990
TrEMBL
other Location (Reliability: 5)
A0A0A0MXY5_RAT
749
0
81756
TrEMBL
other Location (Reliability: 5)
Q52KS1_RAT
780
0
85343
TrEMBL
other Location (Reliability: 1)
A0A8I5ZYA2_RAT
737
0
80431
TrEMBL
other Location (Reliability: 1)
Q6P783_RAT
780
0
85296
TrEMBL
other Location (Reliability: 2)
A0A8I6B663_RAT
788
0
85727
TrEMBL
other Location (Reliability: 1)
C7C5T2_RAT
788
0
85720
TrEMBL
other Location (Reliability: 1)
A0A0G2KBC7_RAT
851
0
93524
TrEMBL
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
380000
413000
-
native PAGE
84500
-
4 * 84500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
4.2 mol phosphate/mol of enzyme in rats treated with 3 doses of isoproterenol, 3 mol phosphate/mol enzyme after dephosphorylation, presence of phosphate groups influences the kinetic properties of PFK-1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, phenyl-Sepharose
-
DEAE Sepharose, Affi-gel blue
-
heat treatment, ammonium sulfate, Cibacron blue F3GA, Sephacryl S-500
-
native enzyme can only be prepared in the presence of proteinase inhibitors
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of full length PFK-A cDNA, i.e. M-type PFK, from islet cDNA library
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 48 h of the chemically induced hypoxia induction of the C6 glioma cells, the PFK1 protein depicts strong up regulation, with no appreciable change in its mRNA levels. The presence of a weak internal ribosome entry site (IRES) element in the 5'UTR of the PFK1 mRNA. The weak IRES element of the PFK1 is strongly up regulated after 48 h of the chemically induced hypoxia, indicative of a possible mechanism responsible for the induction of the PFK1 protein
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
Ozawa, K.
Purification and kinetic properties of phosphofructokinase from dental pulps of rat incisors
Arch. Oral Biol.
30
577-582
1985
Rattus norvegicus
Manually annotated by BRENDA team
Kasten, T.P.; Naqui, D.; Kruep, D.; Dunaway, G.A.
Purification of homogeneous rat phosphofructokinase isozymes with high specific activities
Biochem. Biophys. Res. Commun.
111
462-469
1983
Rattus norvegicus
Manually annotated by BRENDA team
Khoja, S.M.; Beach, N.L.; Kellett, G.L.
The isolation and characterization of phosphofructokinase from the epithelial cells of rat small intestine
Biochem. J.
211
373-379
1983
Rattus norvegicus
Manually annotated by BRENDA team
Brand, I.A.; Soling, H.D.
Zn2+-dependent reversible inactivation of rat liver phosphofructokinase-1. Purification of the inactivating protein and characterization of the inactivation reaction
J. Biol. Chem.
261
5892-5900
1986
Rattus norvegicus
Manually annotated by BRENDA team
Yaney, G.C.; Schultz, V.; Cunningham, B.A.; Dunaway, G.A.; Corkey, B.E.; Tornheim, K.
Phosphofructokinase isozymes in pancreatic islets and clonal beta-cells (INS-1)
Diabetes
44
1285-1289
1995
Rattus norvegicus
Manually annotated by BRENDA team
Ma, Z.; Ramanadham, S.; Kempe, K.; Hu, Z.; Ladenson, J.; Turk, J.
Characterization of expression of phosphofructokinase isoforms in isolated rat pancreatic islets and purified beta cells and cloning and expression of the rat phosphofructokinase-A isoform
Biochim. Biophys. Acta
1308
151-163
1996
Rattus norvegicus
Manually annotated by BRENDA team
Sanchez-Martinez, C.; Aragon, J.J.
Analysis of phosphofructokinase subunits and isozymes in ascites tumor cells and its original tissue, murine mammary gland
FEBS Lett.
409
86-90
1997
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Hagopian, K.; Munday, M.R.
The role of pyruvate dehydrogenase, phosphofructo-1-kinase and acetyl-CoA carboxylase in the regulation of fatty acid synthesis in the lactating rat mammary gland during the starved to re-fed transition
Biochim. Biophys. Acta
1336
474-484
1997
Rattus norvegicus
Manually annotated by BRENDA team
Nicolau, J.; Souza, D.N.; Nunez-Burgos, G.
Regulation of phosphofructokinase-1 on submandibular salivary glands of rats after isoproterenol administration
Arch. Physiol. Biochem.
108
437-443
2000
Rattus norvegicus
Manually annotated by BRENDA team
Ismail, R.; Ul Hussain, M.
The up regulation of phosphofructokinase1 (PFK1) protein during chemically induced hypoxia is mediated by the hypoxia-responsive internal ribosome entry site (IRES) element, present in its untranslated region
Biochimie
139
38-45
2017
Rattus norvegicus (P47858)
Manually annotated by BRENDA team