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Lividomycin Resistance in Staphylococci by Enzymatic Phosphorylation
Author(s) -
Fujio Kobayashi,
Tomoyuki Koshi,
Junji Eda,
Yoko Yoshimura,
Susumu Mitsuhashi
Publication year - 1973
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.4.1.1
Subject(s) - enzyme , escherichia coli , phosphorylation , adenosine triphosphate , microbiology and biotechnology , biochemistry , staphylococcus aureus , ammonium sulfate , staphylococcus , column chromatography , strain (injury) , biology , chemistry , bacteria , chromatography , gene , genetics , anatomy
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 of32 P from γ-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 resistantStaphylococcus 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 fromEscherichia coli carrying an R factor conferring LV resistance, and the phosphorylated product of the drug was also found to be identical with that produced byE. coli carrying an R factor, i.e., 5″-phosphoryl-LV.

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