氨基糖苷类抗生素的酶促修饰：具有广泛特异性的3-N-乙酰基转移酶，其决定对新型氨基糖苷类抗生素阿泊拉霉素的耐药性。
Enzymatic modification of aminoglycoside antibiotics: 3-N-acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin.
作者信息
Davies J, O'Connor S
出版信息
Antimicrob Agents Chemother. 1978 Jul;14(1):69-72. doi: 10.1128/AAC.14.1.69.
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.
摘要
对多个源自动物的含有R质粒的细菌分离株进行检测后发现，存在一种新的氨基糖苷乙酰转移酶（3-N），其底物范围广泛，包括所有双取代的2-脱氧链霉胺抗生素以及新型单取代抗生素阿泊拉霉素。在1-氨基位置被羟基氨基丁酸酰化的抗生素衍生物不会被该酶修饰。
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13C-NMR studies on ribostamycin and its related compounds.核糖霉素及其相关化合物的13C核磁共振研究。
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Gentamicin resistance in strains of Pseudomonas aeruginosa mediated by enzymatic N-acetylation of the deoxystreptamine moiety.铜绿假单胞菌菌株中由脱氧链霉胺部分的酶促N-乙酰化介导的庆大霉素耐药性。
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