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http://purl.uniprot.org/citations/17462573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17462573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17462573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/17462573http://www.w3.org/2000/01/rdf-schema#comment"Butirosin, an aminoglycoside antibiotic produced by Bacillus circulans, bears the unique (S)-4-amino-2-hydroxybutyrate (AHBA) side chain, which protects the antibiotic from several common resistance mechanisms. The AHBA side chain is advantageously incorporated into clinically valuable antibiotics such as amikacin and arbekacin by synthetic methods. Therefore, it is of significant interest to explore the biosynthetic origins of this useful moiety. We report here that the AHBA side chain of butirosin is transferred from the acyl carrier protein (ACP) BtrI to the parent aminoglycoside ribostamycin as a gamma-glutamylated dipeptide by the ACP:aminoglycoside acyltransferase BtrH. The protective gamma-glutamyl group is then cleaved by BtrG via an uncommon gamma-glutamyl cyclotransferase mechanism. The application of this pathway to the in vitro enzymatic production of novel AHBA-bearing aminoglycosides is explored with encouraging implications for the preparation of unnatural antibiotics via directed biosynthesis."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2007.02.005"xsd:string
http://purl.uniprot.org/citations/17462573http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2007.02.005"xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Llewellyn N.M."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Llewellyn N.M."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Spencer J.B."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/author"Spencer J.B."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/pages"379-386"xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/pages"379-386"xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/title"Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/title"Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain."xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17462573http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17462573http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17462573
http://purl.uniprot.org/citations/17462573http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17462573
http://purl.uniprot.org/citations/17462573http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17462573