Gentamicin-adenylyltransferase activity as a cause of gentamicin resistance in clinical isolates of Pseudomonas aeruginosa. Academic Article uri icon

Overview

abstract

  • Gentamicin adenylyltransferase activity was found in extracts of clinical isolates of gentamicin-resistant Pseudomonas aeruginosa. Extracts of one of these isolates, P. aeruginosa POW, inactivated gentamicin in the presence of adenosine 5'-triphosphate. Extracts of strain POW catalyzed the binding of radioactivity from [(14)C]adenine adenosine 5'-triphosphate to gentamicin components, tobramycin, sisomicin, kanamycin A and B and, to a variable degree, streptomycin and spectinomycin. The substrate profile with these agents and other aminocyclitols was similar to that obtained with R factor-mediated gentamicin adenylyltransferase found in Enterobacteriaceae. Adenylylating activity was absent in gentamicin-susceptible mutants of strain POW. Adenylylation may be added to acetylation as an enzymatic mechanism responsible for gentamicin resistance among strains of P. aeruginosa.

publication date

  • June 1, 1974

Research

keywords

  • Anti-Bacterial Agents
  • Drug Resistance, Bacterial
  • Gentamicins
  • Nucleotidyltransferases
  • Pseudomonas aeruginosa

Identity

PubMed Central ID

  • PMC429015

Scopus Document Identifier

  • 17844381910

Digital Object Identifier (DOI)

  • 10.1128/AAC.5.6.565

PubMed ID

  • 15825406

Additional Document Info

volume

  • 5

issue

  • 6