Degradation and reconstruction of moenomycin A and derivatives: Dissecting the function of the isoprenoid chain

Masaatsu Adachi, Yi Zhang, Catherine Leimkuhler, Binyuan Sun, John V. LaTour, Daniel E. Kahne

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)

Abstract

Moenomycin A is the only known natural product that inhibits peptidoglycan biosynthesis by binding the bacterial transglycosylases. We describe a degradation/reconstruction route to manipulate the reducing end of moenomycin A. A comparison of the biological and enzyme inhibitory activity of moenomycin A and an analogue containing a nerol lipid in place of the natural C25 lipid chain provides insight into the role of the moenocinol unit. Our results show that a lipid chain having ten carbons in moenocinol is sufficient for enzyme inhibition, but a longer chain is required for biological acitivity, apparently because the molecule must partition into biological membranes to reach its target in bacterial cells.

Original languageEnglish
Pages (from-to)14012-14013
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number43
DOIs
Publication statusPublished - 2006 Nov 1
Externally publishedYes

ASJC Scopus subject areas

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

Fingerprint Dive into the research topics of 'Degradation and reconstruction of moenomycin A and derivatives: Dissecting the function of the isoprenoid chain'. Together they form a unique fingerprint.

Cite this