| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 25292 | Journal of Biotechnology | 2007 | 7 Pages | 
Abstract
												A strain (S. fradiae ΔurdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae ΔurdQ, in S. fradiae ΔurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae ΔurdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.
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											Authors
												M. Fedoryshyn, M. Nur-e-Alam, L. Zhu, A. Luzhetskyy, J. Rohr, A. Bechthold, 
											