Phosphorylation of Lividomycin by Escherichia coli Carrying an R Factor

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Abstract
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.