Yamaguchi M, Koshi T, Kobayashi F, Mitsuhashi S
Antimicrob Agents Chemother. 1972 Sep;2(3):142-6. doi: 10.1128/AAC.2.3.142.
A lividomycin-phosphorylating enzyme from a lividomycin-resistant strain of Escherichia coli carrying an R factor was partially purified by fractionation with ammonium sulfate and Sephadex G-100 column chromatography. The enzyme inactivated, in the presence of adenosine triphosphate and Mg(2+), several antibiotics having a d-ribose moiety linked to 2-deoxystreptamine, i.e., lividomycin A and B, neomycin, paromomycin, and vistamycin, but did not inactivate the kanamycins, streptomycin, or the gentamicin C components. Chemical studies of the inactivated product suggested that the phosphorylated site of the inactivated lividomycin was the hydroxyl group of the d-ribose moiety.
从携带R因子的抗利福霉素大肠杆菌菌株中分离得到一种利福霉素磷酸化酶,通过硫酸铵分级分离和Sephadex G - 100柱层析进行部分纯化。该酶在三磷酸腺苷和Mg(2+)存在的情况下,能使几种具有与2 - 脱氧链霉胺相连的d - 核糖部分的抗生素失活,即利福霉素A和B、新霉素、巴龙霉素和维斯他霉素,但不能使卡那霉素、链霉素或庆大霉素C组分失活。对失活产物的化学研究表明,失活的利福霉素的磷酸化位点是d - 核糖部分的羟基。