Claim · model-written summary
The cytoplasmic enzyme had a lower pH optimum than the chloroplast enzyme, 7.5 versus 8.5.
- Taxon
- Spinach
Spinacia oleraceat0 - Treatment
- 10 mM Mg2®e0
- Outcome
- pH optimume0
- Direction
- lowere0
- Value
- 7.5e0
- Qualifier
- 8.5 for the chloroplast enzymee0
- Comparator
- chloroplast enzymee0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleSetting
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“assayed with 10 mM Mg2® the pH optimum is lower, (7.5 for the cytoplasmic and 8.5 for the chloroplast enzyme) and the affinity for fructose bisphosphate at the pH optimum is greater.”
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 specifically hydrolyse fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.
- Observation Both spinach enzymes absolutely require Mg2®.
- Association Mg2® concentration did not affect the cytoplasmic enzyme pH optimum.
- 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.