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Literature summary for 3.1.3.11 extracted from

  • Asenjo, J.L.; Ludwig, H.C.; Droppelmann, C.A.; Carcamo, J.G.; Concha, I.I.; Yanez, A.J.; Cardenas, M.L.; Cornish-Bowden, A.; Slebe, J.C.
    Subunit interactions in pig-kidney fructose-1,6-bisphosphatase: binding of substrate induces a second class of site with lowered affinity and catalytic activity (2014), Biochim. Biophys. Acta, 1840, 1798-1807.
    View publication on PubMed
Search for more literature for 3.1.3.11

Protein Variants

Protein Variants Comment Organism
F219W mutation introduced to allow for fluorescence measurements. At concentrations near the Km value, the substrate fructose 1,6-bispohosphate causes a 15% increase in the intrinsic fluorescence of the mutant Sus scrofa
F232W mutation introduced to allow for fluorescence measurements. The fluorescence emission of the mutant is not altered significantly by the substrate Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
D-fructose 2,6-bisphosphate the binding of fructose 1,6-bisphosphate induces the appearance of catalytic sites with lower affinity for substrate and lower catalytic activity. The inhibitor, fructose 1,6-bisphosphate, competes with the substrate for the high-affinity sites. Binding of substrate to the low-affinity sites acts as a stapler that prevents dissociation of the tetramer and hence exchange of subunits, and results in substrate inhibition Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
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-
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Source Tissue

Source Tissue Comment Organism Textmining
kidney
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 Sus scrofa
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
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 Sus scrofa D-fructose 6-phosphate + phosphate
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 ?
additional information binding of the first substrate molecule, in one dimer of the enzyme, produces a conformational change at the other dimer, reducing the substrate affinity and catalytic activity of its subunits Sus scrofa ?
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 ?