The C-glycosyltransferase UrdGT2 is unselective toward D- and L-configured nucleotide-bound rhodinoses

Dirk Hoffmeister, Gerald Dräger, Koji Ichinose, Jürgen Rohr, Andreas Bechthold

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

UrdGT2 is a D-olivosyltransferase from the metabolic pathway of urdamycin A, an angucycline antitumor and antimicrobial drug. The remarkable feature of this biocatalyst is its ability to set up C-glycosidic bonds. Using an in vivo system suitable to deliver the trideoxysugar rhodinose in both D- and L- configuration we could verify that both have been accepted as substrates and attached to the urdamycin polyketide backbone via a C-glycosidic bond. Regardless of the stereochemistry, these C-glycosides served as acceptor for a subsequent glycosylation step to yield the novel urdamycins R and S with di-rhodinosyl side chains at C-9 of the polyketide moiety.

Original languageEnglish
Pages (from-to)4678-4679
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number16
DOIs
StatePublished - Apr 23 2003

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)
  • Biochemistry
  • Colloid and Surface Chemistry

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