Lovering A M, White L O, Reeves D S
Department of Medical Microbiology, Southmead Hospital, Bristol, U.K.
J Antimicrob Chemother. 1987 Dec;20(6):803-13. doi: 10.1093/jac/20.6.803.
An aminoglycoside-acetylating enzyme produced by a strain of Escherichia coli with an unusual resistance phenotype was characterized. This enzyme was found to mono-acetylate apramycin, butirosin, lividomycin and paromomycin and diacetylate ribostamycin and neomycin to give reaction products which were distinguishable by HPLC analysis from those of AAC(2'), AAC(3) and AAC(6') enzymes. The enzyme, however, was not found to acetylate amikacin, fortimicin, geneticin, gentamicin, kanamycin A, netilmicin or tobramycin. The reaction product from the action of this enzyme on apramycin was purified and identified by nuclear magnetic resonance studies as 1-N-acetyl apramycin. The second site at which ribostamycin and neomycin B were modified by this enzyme was not determined but is postulated as the 6'-amino group. It is proposed that this enzyme be named AAC(1).
对一株具有异常耐药表型的大肠杆菌产生的一种氨基糖苷乙酰化酶进行了特性鉴定。发现该酶可使阿泊拉霉素、丁胺卡那霉素、青紫霉素和巴龙霉素单乙酰化，使核糖霉素和新霉素双乙酰化，生成的反应产物通过高效液相色谱分析可与AAC(2')、AAC(3)和AAC(6')酶的产物区分开来。然而，未发现该酶可使阿米卡星、福提霉素、遗传霉素、庆大霉素、卡那霉素A、奈替米星或妥布霉素乙酰化。该酶作用于阿泊拉霉素产生的反应产物经纯化，并通过核磁共振研究鉴定为1-N-乙酰阿泊拉霉素。该酶修饰核糖霉素和新霉素B的第二个位点尚未确定，但推测为6'-氨基。建议将该酶命名为AAC(1)。
