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http://purl.uniprot.org/citations/26361733http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26361733http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26361733http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/26361733http://www.w3.org/2000/01/rdf-schema#comment"The biosynthetic pathway for the cyanogenic glucoside dhurrin in sorghum has previously been shown to involve the sequential production of (E)- and (Z)-p-hydroxyphenylacetaldoxime. In this study we used microsomes prepared from wild-type and mutant sorghum or transiently transformed Nicotiana benthamiana to demonstrate that CYP79A1 catalyzes conversion of tyrosine to (E)-p-hydroxyphenylacetaldoxime whereas CYP71E1 catalyzes conversion of (E)-p-hydroxyphenylacetaldoxime into the corresponding geometrical Z-isomer as required for its dehydration into a nitrile, the next intermediate in cyanogenic glucoside synthesis. Glucosinolate biosynthesis is also initiated by the action of a CYP79 family enzyme, but the next enzyme involved belongs to the CYP83 family. We demonstrate that CYP83B1 from Arabidopsis thaliana cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis. Instead CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure. Numerous microbial plant pathogens are able to detoxify Z-oximes but not E-oximes. The CYP79-derived E-oximes may play an important role in plant defense."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.org/dc/terms/identifier"doi:10.1111/tpj.13023"xsd:string
http://purl.uniprot.org/citations/26361733http://purl.org/dc/terms/identifier"doi:10.1111/tpj.13023"xsd:string
http://purl.uniprot.org/citations/26361733http://purl.org/dc/terms/identifier"doi:10.1111/tpj.13023"xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Bak S."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Bak S."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Olsen C.E."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Olsen C.E."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Moeller B.L."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Moeller B.L."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Blomstedt C.K."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Blomstedt C.K."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Clausen M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Clausen M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Gleadow R.M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Gleadow R.M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Joergensen K."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Joergensen K."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Kannangara R.M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Kannangara R.M."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Motawie M.S."xsd:string
http://purl.uniprot.org/citations/26361733http://purl.uniprot.org/core/author"Motawie M.S."xsd:string