Effect of aminoglycoside concentration on reaction rates of aminoglycoside-modifying enzymes.
Reaction rates of several reference aminoglycoside-modifying enzymes were studied at various substrate concentrations. The resulting concentration-response curves showed wide variation in threshold concentration, in curve slope, in enzyme saturation, and in substrate inhibition. Together, the curves of a defined aminoglycoside panel yielded more specific information for each individual aminoglycoside-modifying enzyme tested than did conventional substrate profiles obtained at a single substrate concentration.
Bongaerts
G P
GP
Department of Medical Microbiology, State University of Leiden, The Netherlands.
Vliegenthart
J S
JS
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D019868:Kanamycin Kinase; D009016:Moraxella / Q000201:enzymology; D009713:Nucleotidyltransferases / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D011532:Providencia / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013211:Staphylococcus aureus / Q000201:enzymology
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase; D010770:Phosphotransferases; D019868:Kanamycin Kinase; D009713:Nucleotidyltransferases; C020565:gentamicin 2''-nucleotidyltransferase