Claim · model-written summary
Both spinach enzymes specifically hydrolyse fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.
- Taxon
- Spinach
Spinacia oleraceat0 - Gene
- enzymese0
- Outcome
- hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphatee0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Both enzymes catalyse specifically the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate and show an absolute requirement for Mg2®.”
t0“Evidence for a Hexosediphosphatase from the Cytoplasm of Spinach Leaves”
Title
Evidence for a Hexosediphosphatase from the Cytoplasm of Spinach Leaves
Erwin Latzko; Gerhard Zimmermann; Urs Feller Biological Chemistry 1974. doi:10.1515/bchm2.1974.355.1.321
Other claims from this paper (10)
- Observation Spinach leaf extracts yielded two peaks of hexosediphosphatase activity.
- Observation Spinach leaves contain chloroplast and cytoplasmic hexosediphosphatases.
- Observation The purified enzyme preparations contained only chloroplast hexosediphosphatase.
- Observation Both spinach enzymes absolutely require Mg2®.
- Association Mg2® concentration did not affect the cytoplasmic enzyme pH optimum.
- Observation The cytoplasmic enzyme had a lower pH optimum than the chloroplast enzyme, 7.5 versus 8.5.
- Observation The cytoplasmic enzyme had greater affinity for fructose bisphosphate than the chloroplast enzyme.
- Intervention effect The cytoplasmic enzyme was not activated by dithiothreitol.
- Intervention effect The cytoplasmic enzyme was not activated by cystamine.
- Intervention effect Adenosine 5'-phosphate inhibited the cytoplasmic enzyme.