Aktivität der Chalkon-Flavanon Isomerase und Akkumulation von phenylpropanoiden Verbindungen in Antheren View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1971-03

AUTHORS

R. Wiermann

ABSTRACT

Chalcone-flavanone isomerase from the anthers of Lilium candidum and Tulipa cv. "Apeldoorn" exhibits a distinct substrate specificity. The enzyme catalyses only the isomerization of 2',4,4',6'-tetrahydroxychalcone, whereas it is not active with 2',4,4'-trihydroxychalcone.During the final stage in the development of the anthers, differing isomerase activities were observed. Maximum enzyme activity was measured at a point when the concentration of chalcones was decreasing rapidly and the concentration of flavonols was increasing. These findings strongly support the suggestion that the isomerase plays an important role in flavonoid metabolism. More... »

PAGES

55-60

Journal

TITLE

Planta

ISSUE

1

VOLUME

102

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00391449

DOI

http://dx.doi.org/10.1007/bf00391449

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035377892

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24482085


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