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Literature summary for 2.7.1.11 extracted from

  • Botha, F.C.; Cawood, M.C.; Small, J.G.C.
    Kinetic properties of the ATP-dependent phosphofructokinase isoenzymes from cucumber seeds (1988), Plant Cell Physiol., 29, 415-421.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
phosphate activation of cytosolic and plastidic isoenzyme Cucumis sativus

Inhibitors

Inhibitors Comment Organism Structure
ATP cytosolic isoenzyme is more sensitive to inhibition at pH 8.0 than pH 7.2, Mg2+ alleviates inhibition Cucumis sativus
MgATP2- cytosolic isozyme Cucumis sativus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol cytosolic and plastidic isoenzyme Cucumis sativus 5829
-
plastid
-
Cucumis sativus 9536
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity Cucumis sativus

Organism

Organism UniProt Comment Textmining
Cucumis sativus
-
2 isoenzymes
-

Purification (Commentary)

Purification (Comment) Organism
2 immunologically distinct isozymes Cucumis sativus

Source Tissue

Source Tissue Comment Organism Textmining
seed germinating Cucumis sativus
-

Substrates and Products (Substrate)

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