Lividomycin Resistance in Staphylococci by Enzymatic Phosphorylation

Overview

Journal Antimicrob Agents Chemother

Publisher American Society for Microbiology

Specialty Pharmacology

Date 1973 Jul 1

PMID 4364938

Citations 3

Authors

F Kobayashi

T Koshi

J Eda

Y Yoshimura

S Mitsuhashi

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

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New plasmid-mediated nucleotidylation of aminoglycoside antibiotics in Staphlococcus aureus.

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