Phosphorylation of lividomycin by Escherichia coli carrying an R factor.
A lividomycin-phosphorylating enzyme from a lividomycin-resistant strain of Escherichia coli carrying an R factor was partially purified by fractionation with ammonium sulfate and Sephadex G-100 column chromatography. The enzyme inactivated, in the presence of adenosine triphosphate and Mg(2+), several antibiotics having a d-ribose moiety linked to 2-deoxystreptamine, i.e., lividomycin A and B, neomycin, paromomycin, and vistamycin, but did not inactivate the kanamycins, streptomycin, or the gentamicin C components. Chemical studies of the inactivated product suggested that the phosphorylated site of the inactivated lividomycin was the hydroxyl group of the d-ribose moiety.
D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D005111:Extrachromosomal Inheritance; D010303:Paromomycin / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism
D010303:Paromomycin; D010770:Phosphotransferases