Claim · model-written summary
Native and recombinant OsTAGG2 showed 4.5–4.7-fold higher activity on salicylic acid glucoside than TAG.
- Taxon
- Rice
Oryza sativat0 - Gene
- OsTAGG2 and rOsTAGG2Pe0
- Outcome
- activities towards salicylic acid β-D-glucosidee0
- Direction
- highere0
- Value
- 4.5-4.7-folde0
- Comparator
- tuberonic acid β-D-glucoside (TAG)e0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentSettingQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Native OsTAGG2 and rOsTAGG2P showed 4.5-4.7-fold higher activities towards salicylic acid β-D-glucoside, an inactive storage-form of salicylic acid, than towards tuberonic acid β-D-glucoside (TAG)”
t0“Rice”
Title
Nami HIMENO; Wataru SABURI; Shinji WAKUTA; et al. Bioscience Biotechnology and Biochemistry 2013. doi:10.1271/bbb.120889
Other claims from this paper (7)
- Observation Recombinant OsTAGG2 yield was 2.1 mg per litre of culture medium.
- Observation Recombinant enzyme specific activity was 182 U/mg, near native enzyme at 171 U/mg.
- Observation E. coli recombinant OsTAGG2 had about threefold lower specific activity than native enzyme.
- Observation Recombinant OsTAGG2 optimum pH was 3.4.
- Observation Recombinant OsTAGG2 optimum temperature was 60 °C.
- Observation Enzyme activity persisted after treatments across pH 3.4–9.8.
- Observation Enzyme activity persisted after heat treatment below 55 °C.