Studies of enzymes that cause resistance to aminoglycosides antibiotics.
Aminoglycoside antibiotics are highly potent, wide-spectrum bactericidals (1, 2). Bacterial resistance to aminoglycosides, however, is a major problem in the clinical use of aminoglycosides. Enzymatic modification of aminoglycosides is the most frequent resistance mode among several resistance mechanisms employed by resistant pathogens (1,3). Three families of aminoglycoside modifying enzymes, O-phosphotransferases, N-acetyltransferases, and N-nucleotidyltransferases, are known to have more than 50 enzymes (1,3,4). In this chapter, determination of enzymatic activity of a single enzyme from each family in the presence and absence of an inhibitor is described.
Serpersu
Engin H
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Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, USA.
Ozen
Can
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Wright
Edward
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D000123:Acetyltransferases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism; D000617:Aminoglycosides / Q000378:metabolism* / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology; D024881:Drug Resistance, Bacterial; D009713:Nucleotidyltransferases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism; D010770:Phosphotransferases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism; D013053:Spectrophotometry / Q000379:methods
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D000123:Acetyltransferases; D010770:Phosphotransferases; D009713:Nucleotidyltransferases