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Literature summary for 2.7.1.11 extracted from

  • Kotlarz, D.; Buc, H.
    Phosphofructokinases from Escherichia coli (1982), Methods Enzymol., 90, 60-70.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
citrate isoenzyme PFK2 Escherichia coli
phosphoenolpyruvate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
D-fructose 6-phosphate pH 8.2, 28°C, PFK2 Escherichia coli
0.05
-
ATP pH 8.2, 28°C, PFK2 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity Escherichia coli
Mg2+ MgATP is the active substrate Escherichia coli
Mn2+ as effective as Mg2+ Escherichia coli
Mn2+ activation Escherichia coli
Mn2+ active substrate: MnATP2-, isoenzyme PFK2 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
4 * 35000, isoenzyme PFK1, tetrahedral arranged subunits, SDS-PAGE Escherichia coli
37000
-
2 * 37000, isoenzyme PFK2, SDS-PAGE Escherichia coli
37000
-
4 * 37000, isoenzyme PFK2, SDS-PAGE in the presence of 1 mM ATP, 5 mM Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K10 or K12 strains Hfr3000, DF1651, DF500, DF443, DF1651B1, AMIR20, PFK1 and PFK2
-

Purification (Commentary)

Purification (Comment) Organism
PFK1, Blue Dextran, heat denaturation, PFK2, Sepharose-Blue Dextran, hydroxyapatite, ammonium sulfate, Blue Dextran, heat denaturation Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
190
-
isoenzyme PFK1 Escherichia coli
205
-
isoenzyme PFK2 Escherichia coli

Storage Stability

Storage Stability Organism
4°C, 65% saturated ammonium sulfate-suspension, at least 2 months, no loss of PFK1 activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-fructose 6-phosphate no activity with glucose 6-phosphate Escherichia coli ADP + D-fructose 1,6-bisphosphate
-
?
ATP + D-fructose 6-phosphate best phosphoryl donors and acceptors of PFK1 and PFK2 Escherichia coli ADP + D-fructose 1,6-bisphosphate
-
?
ATP + D-tagatose 6-phosphate poor substrate for isoenzyme PFK2 Escherichia coli ADP + ?
-
?
CTP + D-fructose 6-phosphate less effective than ATP Escherichia coli CDP + D-fructose 1,6-bisphosphate
-
?
CTP + D-fructose 6-phosphate ITP, GTP or UTP as phosphoryl donors Escherichia coli CDP + D-fructose 1,6-bisphosphate
-
?
dATP + D-fructose 6-phosphate as good as ATP Escherichia coli dADP + D-fructose 1,6-bisphosphate
-
?
GTP + D-fructose 6-phosphate less effective than ATP or ITP, better than UTP or CTP Escherichia coli GDP + D-fructose 1,6-bisphosphate
-
?
ITP + D-fructose 6-phosphate less effective than ATP Escherichia coli IDP + D-fructose 1,6-bisphosphate
-
?
ITP + D-fructose 6-phosphate better than GTP, UTP or CTP Escherichia coli IDP + D-fructose 1,6-bisphosphate
-
?
UTP + D-fructose 6-phosphate less effective than ATP, ITP, GTP, better than CTP Escherichia coli UDP + D-fructose 1,6-bisphosphate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 37000, isoenzyme PFK2, SDS-PAGE Escherichia coli
More 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 Escherichia coli
tetramer 4 * 37000, isoenzyme PFK2, SDS-PAGE in the presence of 1 mM ATP, 5 mM Mg2+ Escherichia coli
tetramer 4 * 35000, isoenzyme PFK1, tetrahedral arranged subunits, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
27 28 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
isoenzyme PFK2, pH-optima at pH 6.5 and pH 8.5 Escherichia coli
8.5
-
isoenzyme PFK2, pH-optima at pH 6.5 and pH 8.5 Escherichia coli