Santanam P, Kayser F H
J Infect Dis. 1976 Aug;134 Suppl:S33-9. doi: 10.1093/infdis/134.supplement_1.s33.
Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin B and C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg++ for activity and is stabilized significantly by dithiothreitol. It is probable that the 4'-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position.
已证明,某些对氨基糖苷类抗生素耐药的表皮葡萄球菌菌株含有一种酶,该酶通过腺苷酸化作用使卡那霉素、新霉素、丁胺卡那霉素、巴龙霉素、庆大霉素A、阿米卡星和妥布霉素失活。这种酶被称为妥布霉素腺苷酸转移酶,发现在pH 5.5时活性最佳。然而,以巴龙霉素或新霉素B和C为底物时,观察到最佳活性的两个pH值(5.5和9.0)。该酶的活性需要Mg++,并被二硫苏糖醇显著稳定。抗生素I环的4'-羟基很可能被腺苷酸化。那些不是该酶底物的氨基糖苷类在相应位置缺少一个羟基。