Claim · model-written summary
The anionic peroxidase preferred feruloyl substrates over caffeoyl, p-coumaryl and syringyl substrates.
- Taxon
- Potato
Solanum tuberosumt0 - Gene
- Peroxidaset1
- Outcome
- substrate preferencee0
- Direction
- preferencee0
- Qualifier
- feruloyl > caffeoyl > p-coumaryl approximately syringyle0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“shows a preference for feruloyl (o-methoxyphenol)-substituted substrates (order of substrate preference: feruloyl > caffeoyl > p-coumaryl approximately syringyl)”
t0“Potato”
t1“Peroxidase”
Title
Biochemical Characterization of the Suberization-Associated Anionic Peroxidase of Potato
Mark A. Bernards; Warren D. Fleming; David B. Llewellyn; et al. PLANT PHYSIOLOGY 1999. doi:10.1104/pp.121.1.135
Other claims from this paper (8)
- Observation The potato wound-associated anionic peroxidase was purified and characterized as a 45-kD class III enzyme.
- Observation The anionic peroxidase localized to suberizing tissues.
- Observation Side chain derivatization had little influence on oxidation.
- Observation Hydroxycinnamates were preferred over their corresponding alcohols.
- Association The substrate specificity pattern was consistent with natural substrate incorporation into potato wound suberin.
- Observation Cationic peroxidases occurred in both suberizing and nonsuberizing potato tissues.
- Observation Cationic peroxidases did not discriminate between hydroxycinnamates and their alcohols.
- Observation The polymer made with purified anionic peroxidase showed substantial C-8 cross-linking while retaining unsaturation.