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. 1973 Jul;4(1):1–5. doi: 10.1128/aac.4.1.1

Lividomycin Resistance in Staphylococci by Enzymatic Phosphorylation

Fujio Kobayashi 1,2, Tomoyuki Koshi 1,2, Junji Eda 1,2, Yoko Yoshimura 1,2, Susumu Mitsuhashi 1,2
PMCID: PMC444495  PMID: 4364938

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 32P from γ-32P-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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