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- W1997145859 abstract "Abstract Two cDNA clones encoding cytochrome P450 enzymes belonging to the CYP79 family have been isolated fromTriglochin maritima. The two proteins show 94% sequence identity and have been designated CYP79E1 and CYP79E2. Heterologous expression of the native and the truncated forms of the two clones inEscherichia coli demonstrated that both encode multifunctional N-hydroxylases catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in T. maritima. This renders CYP79E functionally identical to CYP79A1 from Sorghum bicolor, and unambiguously demonstrates that cyanogenic glucoside biosynthesis in T. maritima and S. bicolor is catalyzed by analogous enzyme systems withp-hydroxyphenylacetaldoxime as a free intermediate. This is in contrast to earlier reports stipulatingp-hydroxyphenylacetonitrile as the only free intermediate in T. maritima.l-3,4-Dihydroxyphenyl[3-14C]Ala (DOPA) was not metabolized by CYP79E1, indicating that hydroxylation of the phenol ring at the meta position, as required for triglochinin formation, takes place at a later stage. In S. bicolor, CYP71E1 catalyzes the subsequent conversion ofp-hydroxyphenylacetaldoxime top-hydroxymandelonitrile. When CYP79E1 from T. maritima was reconstituted with CYP71E1 and NADPH-cytochrome P450 oxidoreductase from S. bicolor, efficient conversion of tyrosine to p-hydroxymandelonitrile was observed." @default.
- W1997145859 created "2016-06-24" @default.
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- W1997145859 date "2000-04-01" @default.
- W1997145859 modified "2023-10-18" @default.
- W1997145859 title "Cloning and Expression of Cytochrome P450 Enzymes Catalyzing the Conversion of Tyrosine to <i>p</i>-Hydroxyphenylacetaldoxime in the Biosynthesis of Cyanogenic Glucosides in <i>Triglochin maritima</i> " @default.
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- W1997145859 doi "https://doi.org/10.1104/pp.122.4.1311" @default.
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