Purification and characterization of aminoglycoside-modifying enzymes from Staphylococcus aureus and Staphylococcus epidermidis.
Several strains of Staphylococcus aureus and Staphylococcus epidermidis, exhibiting characteristic resistance patterns to aminoglycoside antibiotics, were examined. The aminoglycoside-modifying enzymes from these strains were purified by DEAE-Sephadex A-50 chromatography, affinity chromatography, and Sephadex G-100 gel filtration. Three enzymes, a 3'-phosphotransferase III (molecular weight, 31,000; pI 4.1), a bifunctional enzyme having 6'-acetyltransferase and 2"-phosphotransferase (molecular weight, 56,000; pI 4.1) activity, and a 4'4"-adenylytransferase (molecular weight, 34,000; pI 4.7), were isolated from crude extracts of the resistant strains. Aminoglycoside-modifying enzymes with identical enzymatic properties derived from S. aureus and S. epidermidis were also immunologically identical.
D000123:Acetyltransferases / Q000302:isolation & purification; D000617:Aminoglycosides / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D019868:Kanamycin Kinase; D008826:Microbial Sensitivity Tests; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000302:isolation & purification; D010770:Phosphotransferases / Q000302:isolation & purification; D013211:Staphylococcus aureus / Q000201:enzymology*; D013212:Staphylococcus epidermidis / Q000201:enzymology*
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase; D010770:Phosphotransferases; D019868:Kanamycin Kinase; D009713:Nucleotidyltransferases; C020565:gentamicin 2''-nucleotidyltransferase