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http://purl.uniprot.org/citations/11744717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11744717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11744717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11744717http://www.w3.org/2000/01/rdf-schema#comment"Two cDNAs encoding geranyl diphosphate:4-hy-droxybenzoate 3-geranyltransferase were isolated from Lithospermum erythrorhizon by nested PCR using the conserved amino acid sequences among polyprenyl-transferases for ubiquinone biosynthesis. They were functionally expressed in yeast COQ2 disruptant and showed a strict substrate specificity for geranyl diphosphate as the prenyl donor, in contrast to ubiquinone biosynthetic enzymes, suggesting that they are involved in the biosynthesis of shikonin, a naphthoquinone secondary metabolite. Regulation of their expression by various culture conditions coincided with that of geranyltransferase activity and the secondary metabolites biosynthesized via this enzyme. This is the first established plant prenyltransferase that transfers the prenyl chain to an aromatic substrate."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m106387200"xsd:string
http://purl.uniprot.org/citations/11744717http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m106387200"xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Sato F."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Sato F."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Yazaki K."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Yazaki K."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Fujisaki T."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Fujisaki T."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Kunihisa M."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/author"Kunihisa M."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/pages"6240-6246"xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/pages"6240-6246"xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/title"Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum erythrorhizon. Cloning and characterization of a key enzyme in shikonin biosynthesis."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/title"Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum erythrorhizon. Cloning and characterization of a key enzyme in shikonin biosynthesis."xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11744717http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11744717http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11744717