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http://purl.uniprot.org/citations/15026039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15026039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15026039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15026039http://www.w3.org/2000/01/rdf-schema#comment"PdxA (E.C. 1.1.1.262) catalyzes a key step in the biosynthesis of vitamin B(6): the nicotinamide-dependent oxidation of 4-hydroxy-l-threonine-4-phosphate (HTP) to a product tentatively identified as 3-amino-1-hydroxyacetone 1-phosphate (AHAP). To date, the evidence for the formation of AHAP, while self-consistent, has been largely circumstantial, and does not exclude the possibility that the actual product of the enzyme-catalyzed oxidation of HTP might be 2-amino-3-oxo-4-hydroxybutyric acid 4-phosphate which could undergo rapid, non-enzyme-catalyzed decarboxylation once released from the protein. Use of negative ion electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometric analysis (MS-MS) confirms that AHAP is the product of the PdxA-catalyzed reaction."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.org/dc/terms/identifier"doi:10.1016/j.bmcl.2004.01.065"xsd:string
http://purl.uniprot.org/citations/15026039http://purl.org/dc/terms/identifier"doi:10.1016/j.bmcl.2004.01.065"xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/author"Banks J."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/author"Banks J."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/author"Cane D.E."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/author"Cane D.E."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/name"Bioorg. Med. Chem. Lett."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/name"Bioorg. Med. Chem. Lett."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/pages"1633-1636"xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/pages"1633-1636"xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/title"Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-L-threonine-4-phosphate using electrospray ionization mass spectrometry."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/title"Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-L-threonine-4-phosphate using electrospray ionization mass spectrometry."xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15026039http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15026039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15026039
http://purl.uniprot.org/citations/15026039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15026039
http://purl.uniprot.org/citations/15026039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15026039
http://purl.uniprot.org/citations/15026039http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15026039
http://purl.uniprot.org/citations/15026039http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15026039