Gentamicin-adenylyltransferase activity as a cause of gentamicin resistance in clinical isolates of Pseudomonas aeruginosa.
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.
Kabins
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Nathan
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Cohen
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D000255:Adenosine Triphosphate / Q000493:pharmacokinetics; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D002250:Carbon Radioisotopes; D024881:Drug Resistance, Bacterial; D005839:Gentamicins / Q000378:metabolism*; D006801:Humans; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology
D000900:Anti-Bacterial Agents; D002250:Carbon Radioisotopes; D005839:Gentamicins; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases