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Literature summary for 2.7.1.56 extracted from

  • Veiga-da-Cunha, M.; Houyoux, A.; Van Schaftingen, E.
    Overexpression and purification of fructose-1-phosphate kinase from Escherichia coli: Application to the assay of fructose 1-phosphate (2000), Protein Expr. Purif., 19, 48-52.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
 D-Fructose 1-phosphate pH 7.1, 30°C, in the presence of 50 mM KCl Escherichia coli
0.35
-
 ATP pH 7.1, 30°C, in the presence of 5 mM KCl Escherichia coli
0.36
-
 fructose 1-phosphate pH 7.1, 30°C, in the absence of KCl Escherichia coli
0.6
-
 ATP pH 7.1, 30°C, in the presence of 50 mM KCl Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 50 mM, 3fold increase of maximal activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 2 * 34000, recombinant enzyme, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate, Sephadex G25, DEAE-Sepharose Escherichia coli

Storage Stability

Storage Stability Organism
-80°C, 20% glycerol, 2 years, no loss of activity Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 34000, recombinant enzyme, SDS-PAGE Escherichia coli