2"-O-phosphorylation of gentamicin components by a Staphylococcus aureus strain carrying a plasmid.
A wild-type strain of Staphylococcus aureus that inactivates the 4,6-glycosidically linked deoxystreptamine aminoglycoside antibiotics by a plasmid-mediated process was found to harbor two enzymes: an acetyltransferase of the AAC(6') type and a new phosphotranferase specific to the gentamicin components. The target of this last enzyme is the 2''-hydroxyl function of these antibiotics, since one inactivated compound is 2''-(O)-phosphorylsisomicin.
D000123:Acetyltransferases / Q000378:metabolism; D000617:Aminoglycosides / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D004352:Drug Resistance, Microbial; D005839:Gentamicins / Q000378:metabolism*; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010770:Phosphotransferases / Q000378:metabolism; D010957:Plasmids; D013211:Staphylococcus aureus / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D005839:Gentamicins; D000123:Acetyltransferases; D010770:Phosphotransferases