Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin

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HUANG, Fanglu, Dieter SPITELLER, Neil A. KOORBANALLY, Yanyan LI, Nicholas M. LLEWELLYN, Jonathan B. SPENCER, 2007. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. Weinheim : Wiley-VCH Verl.. In: ChemBioChem. 8(3), pp. 283-288. ISSN 1439-4227

@article{Huang2007-02-12Elabo-15471, title={Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin}, year={2007}, doi={10.1002/cbic.200600371}, number={3}, volume={8}, issn={1439-4227}, journal={ChemBioChem}, pages={283--288}, author={Huang, Fanglu and Spiteller, Dieter and Koorbanally, Neil A. and Li, Yanyan and Llewellyn, Nicholas M. and Spencer, Jonathan B.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/15471"> <dc:creator>Spencer, Jonathan B.</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:language>eng</dc:language> <dc:creator>Llewellyn, Nicholas M.</dc:creator> <dc:creator>Spiteller, Dieter</dc:creator> <dc:creator>Huang, Fanglu</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Li, Yanyan</dc:creator> <dcterms:title>Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin</dcterms:title> <dcterms:issued>2007-02-12</dcterms:issued> <dc:publisher>Weinheim : Wiley-VCH Verl.</dc:publisher> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/15471"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-10-20T08:19:09Z</dcterms:available> <dcterms:abstract xml:lang="eng">The proteins Neo-11 and Neo-18 encoded in the neomycin gene cluster (neo) of Streptomyces fradiae NCIMB 8233 have been characterized as glucosaminyl-6′-oxidase and 6′-oxoglucosaminyl:L-glutamate aminotransferase, respectively. The joint activity of Neo-11 and Neo-18 is responsible for the conversion of paromamine to neamine in the biosynthetic pathway of neomycin through a mechanism of FAD-dependent dehydrogenation followed by a pyridoxal-5′-phosphate-mediated transamination. Neo-18 is also shown to catalyze deamination at C-6′′′ of neomycin, thus suggesting bifunctional roles of the two enzymes in the formation of both neosamine rings of neomycin. The product of the btrB gene, a homologue of neo-18 in the butirosin biosynthetic gene cluster (btr) in Bacillus circulans, exhibits the same activity as Neo-18; this indicates that there is a similar reaction sequence in both butirosin and neomycin biosynthesis.</dcterms:abstract> <dcterms:bibliographicCitation>Publ. in: ChemBioChem ; 8 (2007), 3. - S. 283-288</dcterms:bibliographicCitation> <dc:contributor>Spencer, Jonathan B.</dc:contributor> <dc:contributor>Llewellyn, Nicholas M.</dc:contributor> <dc:contributor>Koorbanally, Neil A.</dc:contributor> <dc:contributor>Huang, Fanglu</dc:contributor> <dc:contributor>Li, Yanyan</dc:contributor> <dc:creator>Koorbanally, Neil A.</dc:creator> <dc:contributor>Spiteller, Dieter</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-10-20T08:19:09Z</dc:date> </rdf:Description> </rdf:RDF>

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