Publikation: Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin
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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.
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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. 2007, 8(3), pp. 283-288. ISSN 1439-4227. Available under: doi: 10.1002/cbic.200600371BibTex
@article{Huang2007-02-12Elabo-15471, year={2007}, doi={10.1002/cbic.200600371}, title={Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin}, 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.} }
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