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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The haem-thiolate N-hydroxylase cytochrome P450TYR involved in the biosynthesis of the tyrosine-derived cyanogenic glucoside dhurrin in Sorghum bicolor had recently been isolated. Reconstitution of enzyme activity by insertion of cytochrome P450TYR and NADPH-cytochrome P450-reductase into L-alpha-dilauroylphosphatidylcholine micelles and using tyrosine as substrate results in the formation of p-hydroxyphenylacetaldehyde oxime. Quantitative substrate binding spectra demonstrate that tyrosine and N-hydroxytyrosine are mutually exclusive substrates that bind to the same active site of cytochrome P450TYR. The multifunctionality of cytochrome P450TYR has been confirmed in reconstitution experiments using recombinant cytochrome P450TYR expressed in Escherichia coli. It was earlier reported that an in vitro microsomal system catalyzing all but the last step in the biosynthetic pathway for cyanogenic glucosides exhibits catalytic facilitation (channelling). This observation is explained by the multifunctionality of cytochrome P450TYR. The cytochrome P450TYR sequence represents the first amino acid sequence of a functionally characterized cytochrome P-450 enzyme from a monocotyledonous plant and the first sequence of an N-hydroxylase with high substrate specificity. Multifunctional N-hydroxylases of the cytochrome P-450 type have not previously been reported in living organisms.

drug metabolism and drug interactions

Characterization of Cytochrome P450TYR, A Multifunctional Haem-Thiolate AZ-Hydroxylase Involved in the Biosynthesis of the Cyanogenic Glucoside Dhurrin