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.
|Number of pages
|Journal of Biotechnology
|Published - May 31 2007
Bibliographical noteFunding Information:
This work was supported by the Deutsche Forschungs-gemeinschaft (DFG) grant 6-1 to A.B. and by NIH grant CA 102102 to J.R. We thank Prof. Dr. J. Salas for providing plasmids pLR234Δ7 and pUC18U.
- Deoxysugar biosynthetic enzymes
- Secondary metabolism
- Streptomyces fradiae
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology