Lividomycin resistance in staphylococci by enzymatic phosphorylation.
Enzymatic inactivation of lividomycin (LV) was attempted with nine clinical isolates of staphylococci including LV-susceptible and -resistant strains. LV inactivation and the incorporation into LV of (32)P from gamma-(32)P-adenosine triphosphate were demonstrated in the presence of cell-free extracts from LV-resistant strains but not from LV-susceptible ones. The enzyme was purified approximately 82-fold from a resistant Staphylococcus aureus strain by means of ammonium sulfate fractionation and column chromatography. Some properties of the partially purified LV-phosphorylating enzyme were quite similar to those of an enzyme from Escherichia coli carrying an R factor conferring LV resistance, and the phosphorylated product of the drug was also found to be identical with that produced by E. coli carrying an R factor, i.e., 5''-phosphoryl-LV.
D000255:Adenosine Triphosphate / Q000378:metabolism; D004352:Drug Resistance, Microbial; D010303:Paromomycin / Q000378:metabolism / Q000494:pharmacology*; D010761:Phosphorus Radioisotopes; D010770:Phosphotransferases / Q000378:metabolism; D013210:Staphylococcus / Q000187:drug effects* / Q000201:enzymology
D010761:Phosphorus Radioisotopes; D010303:Paromomycin; D000255:Adenosine Triphosphate; D010770:Phosphotransferases