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. 1978 Jul;14(1):69-72.
doi: 10.1128/AAC.14.1.69.

Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin

J Davies, S O'Connor

Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin

J Davies et al. Antimicrob Agents Chemother. 1978 Jul.

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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References

    1. Antimicrob Agents Chemother. 1974 Sep;6(3):253-62 - PubMed
    1. J Antibiot (Tokyo). 1977 Nov;30(11):1025-7 - PubMed
    1. J Antibiot (Tokyo). 1973 Dec;26(12):717-24 - PubMed
    1. J Org Chem. 1976 Feb 20;41(4):701-2 - PubMed
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