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http://purl.uniprot.org/citations/15911379http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15911379http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15911379http://www.w3.org/2000/01/rdf-schema#comment"Biotin synthase is an S-adenosyl-L-methionine (SAM) radical enzyme that inserts sulfur into dethiobiotin to produce biotin. The reaction proceeds through 5'-deoxyadenosyl radical intermediates that become reduced during the sulfur insertion step to give another product of the reaction, 5'-deoxyadenosine. We report that Escherichia coli strains lacking the 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase encoded by the pfs gene are deficient in biotin synthase activity due to accumulation of 5'-deoxyadenosine, a new substrate of the pfs-encoded nucleosidase. Physiological experiments indicate that lipoic acid synthase, another SAM radical enzyme, is also inhibited by 5'-deoxyadenosine accumulation."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2005.04.012"xsd:string
http://purl.uniprot.org/citations/15911379http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2005.04.012"xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/author"Cronan J.E."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/author"Cronan J.E."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/author"Choi-Rhee E."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/author"Choi-Rhee E."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/pages"589-593"xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/pages"589-593"xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/title"A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/title"A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase."xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/15911379http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/15911379http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15911379
http://purl.uniprot.org/citations/15911379http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15911379
http://purl.uniprot.org/citations/15911379http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15911379
http://purl.uniprot.org/citations/15911379http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15911379
http://purl.uniprot.org/uniprot/P12996http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15911379
http://purl.uniprot.org/uniprot/P0AF12http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15911379