English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Crude protein extracts from the chickpea (Cicer arietinum L.) pathogenic fungus Ascochyta rabiei catalyze the NADPH dependent conversion of the pterocarpan phytoalexins medicarpin and maackiain to 1) 2′-hydroxyisoflavans, 2) 1 a-hydroxypterocarp-1,4-diene-3-one, and 3) 10,2′-dihydroxyisoflav-8-ene-7-one derivatives. A pterocarpan : NADPH oxidoreductase which cleaves the benzylphenyl ether bond of the phytoalexins was purified some 100-fold and partially characterized with regard to its kinetic properties. The oxidoreductase was shown to be specific for NADPH and 3-hydroxypterocarpans. The enzyme appears to be constitutively expressed by A. rabiei.

Partial Characterization of an Enzyme from the Fungus Ascochyta rabiei for the Reductive Cleavage of Pterocarpan Phytoalexins to 2′-Hydroxyisoflavans