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http://purl.uniprot.org/citations/21102469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21102469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21102469http://www.w3.org/2000/01/rdf-schema#comment"The aromatic amino acids L-phenylalanine and L-tyrosine and their plant-derived natural products are essential in human and plant metabolism and physiology. Here we identified Petunia hybrida and Arabidopsis thaliana genes encoding prephenate aminotransferases (PPA-ATs), thus completing the identification of the genes involved in phenylalanine and tyrosine biosyntheses. Biochemical and genetic characterization of enzymes showed that PPA-AT directs carbon flux from prephenate toward arogenate, making the arogenate pathway predominant in plant phenylalanine biosynthesis."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.org/dc/terms/identifier"doi:10.1038/nchembio.485"xsd:string
http://purl.uniprot.org/citations/21102469http://purl.org/dc/terms/identifier"doi:10.1038/nchembio.485"xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Dudareva N."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Dudareva N."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Maeda H."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Maeda H."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Yoo H."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/author"Yoo H."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/name"Nat. Chem. Biol."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/name"Nat. Chem. Biol."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/pages"19-21"xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/pages"19-21"xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/title"Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/title"Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate."xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/21102469http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/21102469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21102469
http://purl.uniprot.org/citations/21102469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21102469
http://purl.uniprot.org/citations/21102469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21102469
http://purl.uniprot.org/citations/21102469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21102469