Enzymatic Modification of Aminoglycoside Antibiotics: 3-N-Acetyltransferase with Broad Specificity that Determines Resistance to the Novel Aminoglycoside Apramycin |
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Authors: | Julian Davies and Sean O''''Connor |
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Affiliation: | 1Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53706;2Lilly Research Laboratories, Indianapolis, Indiana 46206 |
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Abstract: | 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 apramycin. Antibiotic derivatives acylated with hydroxyaminobutyric acid at the 1-amino position were not modified by the enzyme. |
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