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http://purl.uniprot.org/citations/11418103http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11418103http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11418103http://www.w3.org/2000/01/rdf-schema#comment"The deduced polypeptide sequence of open reading frame slr1736 reveals homology to chlorophyll synthase and 1,4-dihydroxy-2-naphthoic acid phytyltransferase in Synechocystis sp. strain PCC 6803. In tocopherol and plastoquinone biosynthesis, a condensation reaction mechanistically similar to that of these two enzymes is performed. To analyze the function of this novel prenyltransferase, a deletion mutant of slr1736 was generated by homologous recombination. The mutant showed a markedly decreased tocopherol content, while plastoquinone levels remained unchanged. Since the aromatic precursor homogentisic acid accumulated in the mutant, the function of the enzyme was proven to be a novel tocopherol phytyltransferase."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)02508-x"xsd:string
http://purl.uniprot.org/citations/11418103http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)02508-x"xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Beyer P."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Beyer P."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Neuhaus G."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Neuhaus G."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Schledz M."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Schledz M."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Seidler A."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/author"Seidler A."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/pages"15-20"xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/pages"15-20"xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/title"A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/title"A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis."xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/volume"499"xsd:string
http://purl.uniprot.org/citations/11418103http://purl.uniprot.org/core/volume"499"xsd:string
http://purl.uniprot.org/citations/11418103http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11418103
http://purl.uniprot.org/citations/11418103http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11418103