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Literature summary for 3.1.3.11 extracted from

  • Tang, G.L.; Wang, Y.F.; Bao, J.S.; Chen, H.B.
    Overexpression in Escherichia coli and characterization of the chloroplast fructose-1,6-bisphosphatase from wheat (2000), Protein Expr. Purif., 19, 411-418.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
guanidine hydrochloride at low concentrations Triticum aestivum
Urea at concentrations lower than 0.8 M Triticum aestivum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Triticum aestivum

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ at high concentration depending on the concentration of Mg2+ Triticum aestivum
K+
-
Triticum aestivum
NH4+
-
Triticum aestivum
Zn2+ the enzyme activity is completely inhibited at concentrations higher than 1 mM in presence of 10 mM Mg2+ Triticum aestivum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.121
-
D-fructose 1,6-bisphosphate pH 8.8, 25°C, recombinant enzyme Triticum aestivum

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Triticum aestivum 9507
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ at low concentrations Triticum aestivum
dithiothreitol the recombinant enzyme is activated Triticum aestivum
Li+ 0.05-0.2 M, 20% activation in presence of 10 mM Mg2+ Triticum aestivum
Mg2+ required Triticum aestivum
Na+ 0.05-0.5 M, 20% activation in presence of 10 mM Mg2+ Triticum aestivum
Zn2+ at low concentrations Triticum aestivum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38900
-
recombinant enzyme Triticum aestivum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O Triticum aestivum the enzyme plays a key role in the Calvin cycle D-fructose 6-phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Triticum aestivum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the recombinant enzyme Triticum aestivum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.8
-
the recombinant enzyme Triticum aestivum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
Triticum aestivum D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O the enzyme plays a key role in the Calvin cycle Triticum aestivum D-fructose 6-phosphate + phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 38900, SDS-PAGE, recombinant enzyme Triticum aestivum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
50 the recombinant enzyme is stable Triticum aestivum
60
-
10% loss of activity Triticum aestivum
70
-
40% loss of activity Triticum aestivum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
22.9
-
D-fructose 1,6-bisphosphate pH 8.8, 25°C, recombinant enzyme Triticum aestivum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1
-
Ca2+ pH 8.8, 25°C, the recombinant enzyme in presence of 2 mM Mg2+ Triticum aestivum
2.5
-
Ca2+ pH 8.8, 25°C, the recombinant enzyme in presence of 10 mM Mg2+ Triticum aestivum