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Literature summary for 3.1.3.11 extracted from

  • Jang, H.K.; Lee, S.W.; Lee, Y.H.; Hahn, T.R.
    Purification and characterization of a recombinant pea cytoplasmic fructose-1,6-bisphosphatase (2003), Protein Expr. Purif., 28, 42-48.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pisum sativum

Inhibitors

Inhibitors Comment Organism Structure
AMP non-competitive inhibition Pisum sativum
D-fructose-2,6-bisphosphate competitive inhibition Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0025
-
D-fructose 1,6-bisphosphate pH 6.6, 25°C, native enzyme Pisum sativum
0.005
-
D-fructose 1,6-bisphosphate pH 6.6, 25°C, Trombin treated enzyme Pisum sativum
0.01
-
D-fructose 1,6-bisphosphate pH 6.6, 25°C, recombinant enzyme Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Pisum sativum 9507
-
cytoplasm
-
Pisum sativum 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
-
Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O Pisum sativum the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm D-fructose 6-phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Pisum sativum Q8RW99
-
-
Spinacia oleracea
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the recombinant enzyme Pisum sativum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.16
-
-
Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
Pisum sativum D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm Pisum sativum D-fructose 6-phosphate + phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 38000, SDS-PAGE Pisum sativum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
optimum of recombinant enzyme Pisum sativum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
the native enzyme is completely inactivated at temperatures higher than 45°C Pisum sativum
55
-
the activity of recombinant enzyme is increased at temperatures higher than 55°C Pisum sativum
65
-
the recombinant enzyme is completely inactivated at temperatures higher than 65°C Pisum sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
the recombinant enzyme Pisum sativum

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 the recombinant enzyme Pisum sativum
7.5 8.2 the native enzyme Pisum sativum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00007
-
D-fructose 2,6-bisphosphate pH 6.6, 25°C, native enzyme Pisum sativum
0.0001
-
D-fructose 2,6-bisphosphate pH 6.6, 25°C, Trombin treated enzyme Pisum sativum
0.00015
-
D-fructose 2,6-bisphosphate pH 6.6, 25°C, recombinant enzyme Pisum sativum
0.12
-
AMP pH 6.6, 25°C, native enzyme Pisum sativum
0.16
-
AMP pH 6.6, 25°C, recombinant enzyme Pisum sativum
0.16
-
AMP pH 6.6, 25°C, Trombin treated enzyme Pisum sativum