Claim · model-written summary
The substrate specificity pattern was consistent with natural substrate incorporation into potato wound suberin.
- Taxon
- potato
Solanum tuberosume0 - Organ / stage
- wound suberine0
- Outcome
- natural substrate incorporation into potato wound suberine0
- Qualifier
- substrate specificity patterne0
Not reportedMaterialGeneCompoundInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The substrate specificity pattern is consistent with the natural substrate incorporation into potato wound suberin”
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 The anionic peroxidase preferred feruloyl substrates over caffeoyl, p-coumaryl and syringyl substrates.
- Observation Side chain derivatization had little influence on oxidation.
- Observation Hydroxycinnamates were preferred over their corresponding alcohols.
- 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.