Open AccessPhosphorylation of Lividomycin by Escherichia coli Carrying an R Factor
Author(s) -
Masatoshi Yamaguchi,
Tomoyuki Koshi,
Fujio Kobayashi,
Susumu Mitsuhashi
Publication year - 1972
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.2.3.142
Subject(s) - escherichia coli , moiety , neomycin , biochemistry , ribose , sephadex , enzyme , chemistry , biology , antibiotics , stereochemistry , gene
A lividomycin-phosphorylating enzyme from a lividomycin-resistant strain ofEscherichia 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 Mg2+ , several antibiotics having ad -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 thed -ribose moiety.