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Literature summary for 3.1.3.11 extracted from

  • Shin, E.H.; Yoo, Y.C.; Lee, S.W.; Hahn, T.R.
    Purification and characterization of a recombinant pea chloroplastic fructose-1, 6-bisphosphatase (2001), Agric. Chem. Biotechnol., 44, 167-172.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol the recombinant enzyme is activated Pisum sativum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
99.98
-
D-fructose 1,6-diphosphate
-
Pisum sativum

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
-
Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
pea
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Pisum sativum
-

Subunits

Subunits Comment Organism
monomer
-
Pisum sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Pisum sativum