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. 1977 Jul;12(1):26–30. doi: 10.1128/aac.12.1.26

2″-O-Phosphorylation of Gentamicin Components by a Staphylococcus aureus Strain Carrying a Plasmid

F Le Goffic *, A Martel 1, N Moreau 1, M L Capmau 1, C J Soussy 1, J Duval 1
PMCID: PMC352148  PMID: 883817

Abstract

A wild-type strain of Staphylococcus aureus that inactivates the 4,6-glycosidically linked deoxystreptamine aminoglycoside antibiotics by a plasmid-mediated process was found to harbor two enzymes: an acetyltransferase of the AAC(6′) type and a new phosphotranferase specific to the gentamicin components. The target of this last enzyme is the 2″-hydroxyl function of these antibiotics, since one inactivated compound is 2″-(O)-phosphorylsisomicin.

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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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