EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.3.11 | 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 |
3.1.3.11 | F232W | mutation introduced to allow for fluorescence measurements. The fluorescence emission of the mutant is not altered significantly by the substrate | Sus scrofa |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.11 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.11 | Sus scrofa | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.11 | kidney | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | 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 | ? | - |
? |