Claim · model-written summary
Cations modulated rice enzyme activity.
- Taxon
- rice
Oryza sativat0 - Gene
- P5C dehydrogenasee1
- Compound
- Cationse0
- Outcome
- enzyme activitye0
Not reportedMaterialOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“rice δ1-pyrroline-5-carboxylate dehydrogenase”
e0“Cations were found to modulate enzyme activity, whereas anion effects were negligible.”
e1“millimolar levels of arginine would increase the affinity of P5C dehydrogenase toward its specific substrate.”
Title
Giuseppe Forlani; Michele Bertazzini; Marco Zarattini; et al. Frontiers in Plant Science 2015. doi:10.3389/fpls.2015.00591
Other claims from this paper (6)
- Observation Rice P5C dehydrogenase was observed as a tetramer.
- Observation The rice enzyme preferentially used NAD(+) as electron acceptor.
- Association Anions had negligible effects on rice enzyme activity.
- Association Several metal ions inhibited rice enzyme activity in the micromolar range.
- Mechanism Arginine inhibited the rice enzyme at higher concentrations through an uncompetitive mechanism relative to P5C.
- Mechanism Millimolar arginine was inferred to increase rice P5C dehydrogenase affinity for its substrate.