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

@article{Kabins1974GentamicinAdenylyltransferaseAA,
  title={Gentamicin-Adenylyltransferase Activity as a Cause of Gentamicin Resistance in Clinical Isolates of Pseudomonas aeruginosa},
  author={Sherwin A. Kabins and Catherine Nathan and S. Cohen},
  journal={Antimicrobial Agents and Chemotherapy},
  year={1974},
  volume={5},
  pages={565 - 570}
}
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… 
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TLDR
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TLDR
The acetyltransferase after DEAE chromatography is stable for many months at -20 degrees C, while the adenylyl transferase after purification is highly unstable; it shows enzymatic activity only in the presence of Mg++.
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TLDR
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Uptake of (methyl-14C)-sisomicin and (methyl-14C)-gentamicin into bacterial cells.
TLDR
In eleven out of the twelve organisms studied employing (methyl-14C)-sisomicin and ( methyl- 14C)-gentamicin, uptake of the former was found higher that that of the latter.
New plasmid-mediated aminoglycoside adenylyltransferase of broad substrate range that adenylylates amikacin
TLDR
The same aminoglycoside 2"-adenylyltransferase was isolated from four gram-negative species which were among a random group of gentamicin-resistant isolates from the same hospital, and genetic experiments clearly established that both enzymes were expressed by a conjugative plasmid.
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