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Literature summary for 2.7.1.11 extracted from

  • 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+ (2011), Arch. Biochem. Biophys., 505, 60-66.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E190Q the mutation drastically diminishes the kinetic affinity of this site for Mg2+ and Mn2+ Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required to obtain full activity of the enzyme Escherichia coli
Mn2+ required to obtain full activity of the enzyme. The affinity for Mn2+ is 13fold higher compared to that of Mg2+ Escherichia coli
additional information Cu2+, Zn2+ and Cd2+ do not significantly support the enzymatic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-fructose 6-phosphate
-
Escherichia coli ADP + D-fructose 1,6-bisphosphate
-
?

Synonyms

Synonyms Comment Organism
Pfk-2
-
Escherichia coli
phosphofructokinase-2
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli
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 Escherichia coli