Enzymatic Modification of Aminoglycoside Antibiotics: 3-N-Acetyltransferase with Broad Specificity that Determines Resistance to the Novel Aminoglycoside Apramycin

Examination of a number of R-plasmid-containing bacterial isolates of animal origin has revealed the presence of a new aminoglycoside acetyltransferase (3-N) with a broad substrate range that includes all the disubstituted 2-deoxystreptamine antibiotics and also the novel monosubstituted antibiotic...

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Библиографические подробности

Опубликовано в::	Antimicrob Agents Chemother
Главные авторы:	Davies, Julian, O'Connor, Sean
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 1978
Предметы:	Biosynthesis; Chemistry; Mechanisms of Action and Resistance
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC352406/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/356726/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.14.1.69
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