Characterization of high-level aminoglycoside resistance in a strain of Streptococcus pneumoniae.
The aminoglycoside phosphotransferase (APH)(3')(5'')-III has been characterized from Streptococcus pneumoniae BM4200, which is resistant to high levels of aminoglycosides. The phosphotransferase was apparently chromosomally-encoded and was responsible for the high-level resistance. The enzyme was not notably pH-dependent, was heterogeneous after isoelectric focusing, with pI values of approximately 4.8 and 5.1, and had an apparent molecular weight of 32 500 after SDS-PAGE.
D000617:Aminoglycosides / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D004352:Drug Resistance, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D019868:Kanamycin Kinase; D010770:Phosphotransferases / Q000032:analysis* / Q000378:metabolism; D011815:R Factors; D013296:Streptococcus pneumoniae / Q000201:enzymology* / Q000235:genetics
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D010770:Phosphotransferases; D019868:Kanamycin Kinase