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Literature summary for 3.1.3.11 extracted from

  • Ashton, A.R.
    A simple procedure for purifying the major chloroplast fructose-1,6-bisphosphatase from spinach (Spinacia oleracea) and characterization of its stimulation by sub-femtomolar mercuric ions (1998), Arch. Biochem. Biophys., 357, 207-224.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
additional information reduction activates several hundred-fold Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Spinacia oleracea 9507
-

Metals/Ions

Metals/Ions Comment Organism Structure
Hg2+ low concentrations stimulate the oxidized enzyme form, but not the reduced enzyme form many hundred-fold. Half-maximal stimulation at 0.2 femtoM: Hg2+ stimulates by binding to an enzyme thiol group, thereby stabilizing the oxidized enzyme in an active conformation Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea P22418
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
 Spinacia oleracea D-fructose 6-phosphate + phosphate
-
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