Effects of altering aminoglycoside structures on bacterial resistance enzyme activities

Keith D. Green, Wenjing Chen, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Aminoglycoside-modifying enzymes (AMEs) constitute the most prevalent mechanism of resistance to aminoglycosides by bacteria. We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased, or completely abolished. We demonstrate that the bifunctional enzyme AAC(3)-Ib/AAC(6′)-Ib′ can diacetylate gentamicin. Since single acetylation does not always inactivate the parent drugs completely, two modifications likely provide morerobust inactivation in vivo.

Original languageEnglish
Pages (from-to)3207-3213
Number of pages7
JournalAntimicrobial Agents and Chemotherapy
Issue number7
StatePublished - Jul 2011

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases


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