[Aminoglycoside-3'-phosphotransferase from Actinomyces fradiae. The identification of its inactivation product].
Neomycin phosphate was obtained as a result of neomycin phosphorylation with aminoglycoside-phosphotransferase from Act. fradiae. It was isolated from the reaction mixture and purified. Successive ion exchange chromatography on columns with Amberlite IRC-50 (NH+4 form), Dowex 1 X 10 (OH- form) and Amberlite CG-50 (NH+4 form) was used for purification of the inactivation product. The findings of the elementary analysis of neomycin phosphate showed the presence of 1 mole of phosphorus per 1 mole of the antibiotic. From the results of the chemical analysis, IR- and NMR-spectrometry neomycin phosphate and neamine phosphate obtained from it by methanolysis were identified as neomycin-3'-phosphate and neamine-3'-phosphate, respectively. The data indicate that the enzyme isolated from Act. fradiae is aminoglycoside-3'-phosphotransferase.
D000617:Aminoglycosides; D002384:Catalysis; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology; D005260:Female; D006863:Hydrogen-Ion Concentration; D009355:Neomycin / Q000037:antagonists & inhibitors; D010085:Oxidative Phosphorylation / Q000187:drug effects; D010770:Phosphotransferases / Q000032:analysis* / Q000494:pharmacology; D013302:Streptomyces / Q000201:enzymology*
D000617:Aminoglycosides; D010770:Phosphotransferases; D009355:Neomycin
Aminoglikozid-3'-fosfotransferaza iz Actinomyces fradiae. Identifikatsiia produkta inaktivatsii.