Claim · model-written summary
The enzyme had a wide pH optimum, especially at high magnesium.
Not reportedTaxonMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Verbatim
e0“There is a wide pH optimum, especially at high Mg(2+).”
Title
Control of Photosynthetic Sucrose Synthesis by Fructose 2,6-Bisphosphate
Mark Stitt; Bernd Herzog; Hans W. Heldt PLANT PHYSIOLOGY 1985. doi:10.1104/pp.79.3.590
Other claims from this paper (19)
- Observation Magnesium was required to activate cytosolic fructose 1,6-bisphosphatase.
- Observation Substrate dependence varied little with pH.
- Intervention effect High magnesium and fructose 1,6-bisphosphate inhibited activity, especially at higher pH.
- Intervention effect Fructose 2,6-bisphosphate inhibited activity across a wide pH range.
- Mechanism Fructose 2,6-bisphosphate lowered maximal activity.
- Mechanism Fructose 2,6-bisphosphate lowered affinity for fructose 1,6-bisphosphate.
- Observation Fructose 2,6-bisphosphate induced sigmoidal substrate saturation kinetics without markedly altering magnesium dependence.
- Observation AMP inhibited competitively against magnesium.
- Observation AMP inhibited noncompetitively against fructose 1,6-bisphosphate.
- Observation With fructose 2,6-bisphosphate present, AMP inhibition depended on fructose 1,6-bisphosphate.
- Observation With AMP present, fructose 2,6-bisphosphate inhibition depended on magnesium.
- Observation Fructose 6-phosphate inhibited competitively against fructose 1,6-bisphosphate.
- Observation Phosphate inhibited competitively against fructose 1,6-bisphosphate.
- Observation Fructose 2,6-bisphosphate did not affect phosphate inhibition.
- Observation Fructose 2,6-bisphosphate weakened inhibition by fructose 6-phosphate.
- Observation Dihydroxyacetone phosphate inhibited noncompetitively against substrate and magnesium.
- Observation Hydroxypyruvate inhibited noncompetitively against substrate and magnesium.
- Observation Dihydroxyacetone phosphate acted as an activator with fructose 2,6-bisphosphate by decreasing substrate S(0.5).
- Observation Hydroxypyruvate acted as an activator with fructose 2,6-bisphosphate by decreasing substrate S(0.5).