Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin

Antimicrob Agents Chemother. 1978 Jul;14(1):69-72. doi: 10.1128/AAC.14.1.69.


Examination of a number of R-plasmid-containing bacterial isolates of animal origin has revealed the presence of a new aminoglycoside acetyltransferase (3-N) with a broad substrate range that includes all the disubstituted 2-deoxystreptamine antibiotics and also the novel monosubstituted antibiotic apramycin. Antibiotic derivatives acylated with hydroxyaminobutyric acid at the 1-amino position were not modified by the enzyme.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetyltransferases / physiology*
  • Anti-Bacterial Agents / pharmacology*
  • Drug Resistance, Microbial
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Nebramycin / analogs & derivatives
  • Nebramycin / metabolism
  • Nebramycin / pharmacology*


  • Anti-Bacterial Agents
  • Nebramycin
  • Acetyltransferases