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Literature summary for 3.1.3.11 extracted from

  • Babul, J.; Guixe, V.
    Fructose bisphosphatase from Escherichia coli. Purification and characterization (1983), Arch. Biochem. Biophys., 225, 944-949.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
AMP 50% inhibition at 0.015 mM Escherichia coli
fructose 1,6-diphosphate substrate inhibition above 0.05 M Escherichia coli
phosphoenolpyruvate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
fructose 1,6-diphosphate
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mn2+ no activation Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
4 * 40000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
Escherichia coli D-fructose 6-phosphate + phosphate
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 40000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli