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http://purl.uniprot.org/citations/20883697http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20883697http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20883697http://www.w3.org/2000/01/rdf-schema#comment"In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2010.09.037"xsd:string
http://purl.uniprot.org/citations/20883697http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2010.09.037"xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Giustini C."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Giustini C."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Graindorge M."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Graindorge M."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Matringe M."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Matringe M."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Curien G."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Curien G."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Kraut A."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Kraut A."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Jacomin A.C."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/author"Jacomin A.C."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/pages"4357-4360"xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/pages"4357-4360"xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/title"Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis."xsd:string
http://purl.uniprot.org/citations/20883697http://purl.uniprot.org/core/title"Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis."xsd:string