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Information on EC 2.7.1.11 - 6-phosphofructokinase and Organism(s) Escherichia coli and UniProt Accession P0A796
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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: Escherichia coli
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, 
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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
-
-
-
-
Pfk-2
PFK1
-
-
-
-
PFK2
-
-
-
-
phospho-1,6-fructokinase
-
-
-
-
phosphofructokinase
-
-
-
-
phosphofructokinase 1
-
-
-
-
phosphofructokinase-2
phosphohexokinase
-
-
-
-
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
1-carboxymethyl-ATP + D-fructose 6-phosphate
1-carboxymethyl-ADP + D-fructose 1,6-bisphosphate
90% of activity with with ATP
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
60fold lower kcat than with fructose 6-phosphate
-
?
ATP + sedoheptulose 7-phosphate
ADP + sedoheptulose 1,7-bisphosphate
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + 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
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-tagatose 6-phosphate
ADP + ?
-
poor substrate for isoenzyme PFK2
-
-
?
TTP + D-fructose 6-phosphate
TDP + 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
-
-
-
?
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
-
?
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
-
?
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
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
-
less effective than ATP or ITP, better than 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
-
less effective than ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
-
better than GTP, UTP or CTP
-
?
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
-
?
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
-
first step in glycolysis
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
additional information
-
Cu2+, Zn2+ and Cd2+ do not significantly support the enzymatic activity
Mg2+
-
required for activity
Mn2+
-
required to obtain full activity of the enzyme. The affinity for Mn2+ is 13fold higher compared to that of Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
inhibition of fructose 1-phosphate phosphorylation above 0.08 mM ATP
D-fructose 6-phosphate
inhibition occurs at low concentrations of fructose 6-phosphate
additional information
-
not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.096
D-fructose 6-phosphate
pH 7.2, 30°C, cosubstrate gamma-thio-ATP
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
0.012
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.049
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.117
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.007
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
0.018
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
0.037
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
additional information
additional information
-
kinetic data of various organism
-
additional information
additional information
-
kinetic properties of dansylated enzyme
-
additional information
additional information
-
effects of temperature on kinetic properties
-
additional information
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
additional information
-
kinetic model of phosphofructokinase-1
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat increases with pH, addition of GDP increases Kcat at constant pH
-
0.016
D-fructose 6-phosphate
pH 7.2, 30°C, cosubstrate gamma-thio-ATP
0.037
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.24
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
9
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
62
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
44
D-fructose 6-phosphate
in the presence of 0.5 mM MgATP2-, at pH 8.2 and 25°C
60
D-fructose 6-phosphate
in the presence of 0.1 mM MgATP2-, at pH 8.2 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
180
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
5200
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
7000
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a knockout of 6-phosphofructokinase I and blocking of the Entner-Doudoroff pathway efficiently increased riboflavin production in Escherichia coli
metabolism
in Escherichia coli, the phosphorylation of fructose-6-phosphate is catalyzed by two isozymes, 6-phosphofructokinase I (pfkA) and 6-phosphofructokinase II (pfkB). More than 90% of the phosphofructokinase activity relies on pfkA. A knockout of 6-phosphofructokinase I and blocking of the Entner-Doudoroff pathway efficiently increased riboflavin production in Escherichia coli
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
-
4 * 35000, isoenzyme PFK1, tetrahedral arranged subunits, SDS-PAGE
36500
-
x * 36500, sedimentation equilibrium centrifugation in 6 M guanidine
37000
37000
-
4 * 37000, isoenzyme PFK2, SDS-PAGE in the presence of 1 mM ATP, 5 mM Mg2+
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
-
4 * 37000, isoenzyme PFK2, SDS-PAGE in the presence of 1 mM ATP, 5 mM Mg2+
tetramer
-
4 * 35000, isoenzyme PFK1, tetrahedral arranged subunits, SDS-PAGE
additional information
-
in the absence of substrates PFK2 is a dimer, in the presence of high concentrations of ATP or ATP analogs, this dimer aggregates into a tetramer, aggregation is reversed by adddition of fructose 6-phosphate
additional information
the isolated subunit has overall higher solvent accessibility than the native dimer, with the exception of residues 240-309, corresponding to most of the beta-meander module. The hydrophobic core of the isolated monomer of Pfk2 is solvent-penetrated in native conditions and the beta-meander module is not affected by monomerizing mutations
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
concentrated PFK solution is mixed with solutions containing fructose 6-phosphate, ADP and 2-methyl-2,4-pentanediol in a glass tube to a final concentration of 4 mg/ml PFK, 50% 2-methyl-2,4-pentanediol, 0.2 mM fructose 6-phosphate, 5 or 10 mM ATP, 100 mM Tris-HCl, pH 8.3, 5 mM MgCl2, 2.4 mM dithiothreitol, and 2.4 mM EDTA, crystal structure of PFK complexed with fructose 1,6-bisphosphate, ATP/Mg2+ and ADP/Mg2+ at 2.4 A resolution
-
crystals are obtained from solutions containing 10 mg/ml PFK, 14% polyethylene glycol 6000, 1-1.1 M NaCl, 50 mM Tris-HCl, pH 7.7-7.9, crystal structure of PFK in the absence of ligands at 2.4 A resolution
-
isozyme Pfk-2 in complex with D-fructose 6-phosphate, hanging drop vapor diffusion method, using 23% (w/v) PEG 4000, 100 mM sodium acetate, pH 4.75, and 200 mM ammonium acetate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R25S
not activated by GDP, pattern of ATP inhibition nearly identical to wild-type
E190Q
-
the mutation drastically diminishes the kinetic affinity of this site for Mg2+ and Mn2+
H249E
-
ability to be allosterically regulated is retained, inhibition by phosphoenol pyruvate is lost
I126A
-
600fold lower affinity for fructose 6-phosphate than wild-type, modestly lower Kcat than wild-type, greater ATP inhibition at pH 6.0 and 7.0 than at pH 8.0
L93A
single-point mutant, constructed to destabilize the interface of isoform Pfk2. The mutant is an inactive monomer at protein concentrations below 30 microM. Active dimer formation can be induced by increasing the protein concentration and by addition of its substrate fructose-6-phosphate. Unfolding occurs noncooperatively and the isolated subunit is partially unstructured and marginally stable
R252E
-
allosteric response to MgATP2- is lost, inhibition by phosphoenol pyruvate is lost
R252Q
-
50fold decrease in Kcat, 1600fold increase in Km for fructose 6-phosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 M Tris-HCl buffer, pH 8, 2 mM MgCl2, 1 mM EDTA, 14 mM 2-mercaptoethanol, 10% v/v glycerol, 20% loss of activity within 3 weeks
-
4°C, 65% saturated ammonium sulfate-suspension, at least 2 months, no loss of PFK1 activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, acetone, QAE-Sephadex, acid, QAE-Sephadex, hydroxyapatite
-
PFK1, Blue Dextran, heat denaturation, PFK2, Sepharose-Blue Dextran, hydroxyapatite, ammonium sulfate, Blue Dextran, heat denaturation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
Kruger, N.J.; Hammond, J.B.W.; Burrell, M.M.
Molecular characterization of four forms of phosphofructokinase purified from potato tuber
Arch. Biochem. Biophys.
267
690-700
1988
Escherichia coli, Solanum acaule, Solanum commersonii, Solanum megistacrolobum, Solanum tuberosum, Escherichia coli DF1020
Kotlarz, D.; Buc, H.
Phosphofructokinases from Escherichia coli
Methods Enzymol.
90
60-70
1982
Escherichia coli
Kemerer, V.F.; Griffin, C.C.; Brand, L.
Phosphofructokinase from Escherichia coli
Methods Enzymol.
42C
91-98
1975
Escherichia coli
-
Deville-Bonne, D.; Bourgain, F.; Garel, J.R.
pH Dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli
Biochemistry
30
5750-5754
1990
Escherichia coli
Zheng, R.L.; Kemp, R.G.
The mechanism of ATP inhibition of wild type and mutant phosphofructo-1-kinase from Escherichia coli
J. Biol. Chem.
267
23640-23645
1992
Escherichia coli, Escherichia coli DF1020
Kruger, N.J.
Effects of temperature on the kinetic properties of phosphofructokinase from Escherichia coli
Biochem. Soc. Trans.
17
760-761
1989
Escherichia coli, Escherichia coli DF1020
-
Shirakihara, Y.; Evans, P.R.
Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
J. Mol. Biol.
204
973-994
1988
Geobacillus stearothermophilus, Escherichia coli, Escherichia coli DF1020
Rypniewski, W.R.; Evans, P.R.
Crystal structure of unliganded phosphofructokinase from Escherichia coli
J. Mol. Biol.
207
805-821
1989
Escherichia coli
Fenton, A.W.; Paricharttanakul, N.M.; Reinhart, G.D.
Identification of Substrate Contact Residues Important for the Allosteric Regulation of Phosphofructokinase from Escherichia coli
Biochemistry
42
6453-6459
2003
Escherichia coli
Zheng, R.L.; Kemp, R.G.
Phosphofructo-1-kinase: role of charge neutralization in the active site
Biochem. Biophys. Res. Commun.
214
765-770
1995
Escherichia coli
Wang, X.; Kemp, R.G.
Identification of residues of Escherichia coli phosphofructokinase that contribute to nucleotide binding and specificity
Biochemistry
38
4313-4318
1999
Escherichia coli (P0A796), Escherichia coli
Wang, X.; Kemp, R.G.
Reaction path of phosphofructo-1-kinase is altered by mutagenesis and alternative substrates
Biochemistry
40
3938-3942
2001
Escherichia coli (P0A796), Escherichia coli
Peskov, K.; Goryanin, I.; Demin, O.
Kinetic model of phosphofructokinase-1 from Escherichia coli
J. Bioinform. Comput. Biol.
6
843-867
2008
Escherichia coli
Rivas-Pardo, J.; Caniuguir, A.; Wilson, C.; Babul, J.; Guixe, V.
Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+
Arch. Biochem. Biophys.
505
60-66
2011
Escherichia coli
Cabrera, R.; Baez, M.; Pereira, H.M.; Caniuguir, A.; Garratt, R.C.; Babul, J.
The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: Kinetic and structural analysis of the allosteric ATP inhibition
J. Biol. Chem.
286
5774-5783
2011
Escherichia coli (P06999), Escherichia coli
Ramirez-Sarmiento, C.A.; Baez, M.; Zamora, R.A.; Balasubramaniam, D.; Babul, J.; Komives, E.A.; Guixe, V.
The folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutant
Biophys. J.
108
2350-2361
2015
Escherichia coli (P06999)
Liu, S.; Kang, P.; Cui, Z.; Wang, Z.; Chen, T.
Increased riboflavin production by knockout of 6-phosphofructokinase I and blocking the Entner-Doudoroff pathway in Escherichia coli
Biotechnol. Lett.
38
1307-1314
2016
Escherichia coli (P0A796), Escherichia coli, Escherichia coli K12 (P0A796)
Koendjbiharie, J.G.; Hon, S.; Pabst, M.; Hooftman, R.; Stevenson, D.M.; Cui, J.; Amador-Noguez, D.; Lynd, L.R.; Olson, D.G.; van Kranenburg, R.
The pentose phosphate pathway of cellulolytic clostridia relies on 6-phosphofructokinase instead of transaldolase
J. Biol. Chem.
295
1867-1878
2020
Pseudoclostridium thermosuccinogenes, Escherichia coli (P0A796), Escherichia coli, Escherichia coli BW25113 (P0A796)
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