Purification and Properties of Dihydrostreptomycin-Phosphorylating Enzyme from Pseudomonas aeruginosa

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The distribution of the dihydrostreptomycin (DHSM)-phosphorylating enzyme was investigated using DHSM-resistant strains of Pseudomonas aeruginosa, indicating that this enzyme was demonstrated from all of 7 DHSM-resistant strains examined but not from a DHSM-sensitive one. The DHSM-phosphorylating enzyme was isolated from P. aeruginosa TI-13 and purified about 205-fold using Sephadex G-75 and DEAE-Sephadex A-50 column chromatography. The optimal pH for the DHSM-inactivation was around 10.0. and both adenosinetriphosphate (ATP) and Mg++ were required for the inactivating reaction. It was found that this cnzyme inactivated only DHSM but not other aminoglycosidic antibioties such as kanamycin, aminodeoxykanamycin, neomycin, paromomycin, lividomycin and gentamicin.
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