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Information on EC 2.7.1.11 - 6-phosphofructokinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P16862
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2.7.1.11 6-phosphofructokinaseIUBMB 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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Word Map
- 2.7.1.11
- citrate
- glycogen
- amp
- glucose-6-phosphate
- 2,6-bisphosphate
- aldolase
- phosphorylase
- phosphoenolpyruvate
- erythrocyte
- pentose
- glucokinase
-
gluconeogenesis
- malate
- creatine
- hexose
- glyceraldehyde-3-phosphate
- phosphoglycerate
- fructose-2,6-bisphosphate
- enolase
- fructose-1,6-bisphosphatase
-
gluconeogenic
-
vastus
-
carboxykinase
- 6-phosphogluconate
- lateralis
- 6-phosphofructo-2-kinase
-
phosphoglucose
- triose
- phosphoglucomutase
- pfkfb3
- soleus
-
1,6-bisphosphatase
- mgatp
- phosphocreatine
- fbpase
-
m-type
- fructose-1,6-diphosphate
- myoglobinuria
-
bisphosphatase
- glycogenosis
-
2.7.1.1
- 1,6-diphosphate
-
liver-type
-
entner-doudoroff
- 2,3-diphosphoglycerate
- 3-hydroxyacyl-coa
- mcardle
- synthesis
-
heterotropic
- biotechnology
- analysis
-
glycogenolytic
- myophosphorylase
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
phosphofructokinase, 6-phosphofructokinase, 6-phosphofructo-1-kinase, pfk-1, phosphofructokinase-1, pfk-m, phosphofructokinase 1, atp-dependent phosphofructokinase, atp-pfk, pfk-l, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
PFK1
PFK2
-
-
-
-
phospho-1,6-fructokinase
-
-
-
-
phosphofructokinase
-
-
-
-
phosphofructokinase 1
-
-
-
-
phosphohexokinase
-
-
-
-
PFK1
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructofuranose 6-phosphate = ADP + beta-D-fructofuranose 1,6-bisphosphate
mechanism
-
ATP + beta-D-fructofuranose 6-phosphate = ADP + beta-D-fructofuranose 1,6-bisphosphate
K-type allosteric enzyme, ordered sequential mechanism at pH 6.4
-
ATP + beta-D-fructofuranose 6-phosphate = ADP + beta-D-fructofuranose 1,6-bisphosphate
structure-oriented allosteric four-state model describing substrate and effector actions on PFK
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -
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
9001-80-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
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
-
-
-
?
additional information
?
-
-
structure of the ATP-bound state of phosphofructokinase determined by cryo-electron microscopy
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 2,6-bisphosphate
-
strong positive allosteric action on PFK
NH4+
-
increases maximum activity of PFK and the affinity of PFK to fructose 6-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
optimum depends on the ATP and fructose 6-phosphate concentration
additional information
additional information
-
pH-optimum depends on nucleoside triphosphate substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
112000
-
alpha2beta4alpha2 or beta2alpha4beta2, 4 * 118000 + 4 * 112000, SDS-PAGE
118000
-
alpha2beta4alpha2 or beta2alpha4beta2, 4 * 118000 + 4 * 112000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
octamer
-
alpha2beta4alpha2 or beta2alpha4beta2, 4 * 118000 + 4 * 112000, SDS-PAGE
octamer
-
the structure of Pfk1 (beta2alpha4beta2) in the T-state (generated by incubating the enzyme with saturating amounts of Mg-ATP) is determined by cryo-electron microscopy
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 6-10% (w/v) PEG 4000 and 0.2 mM sodium acetate in 0.1 M 4-morpholineethanesulfonic acid buffer (pH 6.0)
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fructose 6-phosphate, ATP or ammonium sulfate stabilizes during dialysis and storage at pH 6-9
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, dilute enzyme solution in 5 mM imidazole-HCl buffer, pH 7, 1 mM D-fructose 6-phosphate, 5 mM 2-mercaptoethanol, 0.5 mM PMSF, 6 h, 20% loss of activity
-
4°C, concentrated enzyme solution, 50 mM potassium phosphate buffer, pH 7, 1 mM EDTA, 5 mM 2-mercaptoethanol, 0.5 mM PMSF, 1 mM fructose 6-phosphate, several months
-
4°C, fructose 6-phosphate, ATP or NH4+ stabilizes at pH-values from 6 to 9
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PEG 6000 precipitation at 3.5% and 14% (w/v) and Cibacron Blue F3G-A Sephadex G 100 gel filtration
acetone, protamine sulfate, Matrex-blue A, Sephacryl S-300, very rapid purification
-
ammonium sulfate, Cibacron Blue F3G-A, gel filtration, ion-exchange
-
protamine sulfate, ammonium sulfate, acetone, ammonium sulfate, Bio-Gel, DEAE-cellulose, hydroxyapatite
-
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
-
Hofmann, E.; Kopperschlger, G.
Phosphofructokinase from yeast
Methods Enzymol.
90
49-60
1982
Saccharomyces cerevisiae
Stellwagen, E.; Wilgus, H.
Phosphofructokinase from rabbit skeletal muscle
Methods Enzymol.
42C
78-85
1975
Saccharomyces cerevisiae
Welch, P.; Scopes, R.K.
Rapid purification and crystallization of yeast phosphofructokinase
Anal. Biochem.
112
154-157
1981
Saccharomyces cerevisiae
Barcena, M.; Radermacher, M.; Baer, J.; Kopperschlaeger, G.; Ruiz, T.
The structure of the ATP-bound state of S. cerevisiae phosphofructokinase determined by cryo-electron microscopy
J. Struct. Biol.
159
135-143
2007
Saccharomyces cerevisiae
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
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