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. 1974 Jun;5(6):565–570. doi: 10.1128/aac.5.6.565

Gentamicin-Adenylyltransferase Activity as a Cause of Gentamicin Resistance in Clinical Isolates of Pseudomonas aeruginosa

S Kabins 1, C Nathan 1, S Cohen 1
PMCID: PMC429015  PMID: 15825406

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 [14C]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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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