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. 1974 Jun;5(6):558–561. doi: 10.1128/aac.5.6.558

Enzymatic Inactivation of a New Aminoglycoside Antibiotic, Sisomicin, by Resistant Strains of Pseudomonas aeruginosa

K O'Hara a,1, M Kono a,1, S Mitsuhashi a
PMCID: PMC429013  PMID: 15825404

Abstract

The antibacterial activity of sisomicin (SS), a new aminoglycoside antibiotic active toward clinical isolates of Pseudomonas aeruginosa, was determined and compared with that of the gentamicin C complex. Both drugs were effective against these strains and showed almost the same antibacterial activity. A few strains were found to be resistant to SS. The antibiotic was inactivated by a cell-free extract from the SS-resistant strains due to acetylation of the drug. Comparative studies of the inactivation of the drugs which lack a 6′-amino group in the amino sugar linked to 2-deoxystreptamine strongly suggested that SS inactivation was due to acetylation of the 6′-amino group of the 4′,5′-didehydropurpurosamine moiety.

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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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