Surprising production of a new urdamycin derivative by S. fradiae Delta urdQ/R

J Biotechnol. 2007 May 31;130(1):32-8. doi: 10.1016/j.jbiotec.2007.02.018. Epub 2007 Feb 28.

Abstract

A strain (S. fradiae Delta urdQ/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 Delta urdQ, in S. fradiae DeltaurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae Delta urdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminoglycosides / chemistry
  • Aminoglycosides / metabolism
  • Anthraquinones / chemistry
  • Anthraquinones / metabolism
  • Biotechnology*
  • Gene Expression Regulation, Bacterial
  • Glycosylation
  • Macrolides / chemistry
  • Macrolides / metabolism
  • Mutation
  • Plasmids
  • Streptomyces / classification
  • Streptomyces / genetics*
  • Streptomyces / metabolism*

Substances

  • Aminoglycosides
  • Anthraquinones
  • Macrolides
  • urdamycin B
  • kerriamycin B