Claim · model-written summary
OsSNAT2 activity was threefold higher than OsSNAT1 activity.
- Taxon
- rice
Oryza sativae1 - Gene
- OsSNAT2e0
- Outcome
- enzyme activitye0
- Direction
- highere0
- Value
- threefolde0
- Comparator
- OsSNAT1e0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentSettingQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The enzyme activity of OsSNAT2 was threefold higher than that of OsSNAT1”
e1“from rice”
Title
Yeong Byeon; Hyoung Yool Lee; Kyoungwhan Back Journal of Pineal Research 2016. doi:10.1111/jpi.12339
Other claims from this paper (13)
- Observation OsSNAT2 was cloned from rice.
- Observation OsSNAT2 and OsSNAT1 proteins had 39% sequence identity.
- Observation OsSNAT2 and OsSNAT1 proteins had 60% sequence similarity.
- Observation Purified recombinant OsSNAT2 had a Km of 371 μm.
- Observation Purified recombinant OsSNAT2 had a Vmax of 4700 pmol/min/mg protein.
- Observation OsSNAT2 enzyme activity was optimal at 45°C.
- Observation OsSNAT2 localized to cytoplasm and chloroplasts.
- Intervention effect Melatonin severely inhibited OsSNAT2 in vitro activity.
- Intervention effect Melatonin did not inhibit rice OsSNAT1 activity.
- Observation OsSNAT2 activity was 232-fold lower than sheep OaSNAT activity.
- Observation Cadmium treatment and melatonin induction similarly suppressed OsSNAT1 and OsSNAT2 transcripts in rice leaves.
- Observation Phylogenetic analysis placed OsSNAT1 and OsSNAT2 as distantly related.
- Mechanism The authors infer independent evolution of OsSNAT1 and OsSNAT2 from Cyanobacteria before endosymbiosis.