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http://purl.uniprot.org/citations/15489164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15489164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15489164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15489164http://www.w3.org/2000/01/rdf-schema#comment"Thiamin-pyrophosphate is an essential cofactor in all living systems. The biosynthesis of both the thiazole and the pyrimidine moieties of this cofactor involves new biosynthetic chemistry. Thiazole-phosphate synthase (ThiG) catalyses the formation of the thiazole moiety of thiamin-pyrophosphate from 1-deoxy-D-xylulose-5-phosphate (DXP), dehydroglycine and the sulfur carrier protein (ThiS), modified on its carboxy terminus as a thiocarboxylate (ThiS-thiocarboxylate). Thiazole biosynthesis is initiated by the formation of a ThiG/DXP imine, which then tautomerizes to an amino-ketone. In this paper we study the sulfur transfer from ThiS-thiocarboxylate to this amino-ketone and trap a new thioenolate intermediate. Surprisingly, thiazole formation results in the replacement of the ThiS-thiocarboxylate sulfur with an oxygen from DXP and not from the buffer, as shown by electrospray ionization Fourier transform mass spectrometry (ESI-FTMS) using (18)O labeling of the 13C-, 15N-depleted protein. These observations further clarify the mechanism of the complex thiazole biosynthesis in bacteria."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2004.08.009"xsd:string
http://purl.uniprot.org/citations/15489164http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2004.08.009"xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Begley T.P."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Begley T.P."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Dorrestein P.C."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Dorrestein P.C."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"McLafferty F.W."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"McLafferty F.W."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Zhai H."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/author"Zhai H."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/pages"1373-1381"xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/pages"1373-1381"xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/title"The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/title"The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS."xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/15489164http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/15489164http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15489164