Butirosin inactivated

A newly Isolated, plasmid-determined acetyl transferase [AAC(3)-III] inactivates most aminoglycosides, including gentamicin and apramycln, but not butirosin, amikacin or fortlmlcin. Earlier data had indicated no cross-resistance of apramycln with other aminoglycosides. " A broad-... 

Deoxykanamycin A (/ 73), in contrast to kanamydn A, is not phosphoryl-ated by 3 -0-phosphotransferase II, while the 3 -0-phosphotransferase I producing strains show resistance. Therefore, the 4 -hydroxyl group must be involved in the binding with the enzyme phosphotransferase II. By a study of the effect of the 4 -deoxygenation with neamine, l-N-HABA-neamine, ribostamycin and butirosin, it could be established that the inactivating reaction of the phosphotransferase II can only be prevented, if the 1 -amino function is substituted by an amino acid side chain (HABA). 

The inactivated butirosin A darkens at 217-221°. The empirical formula of butirosin A monophosphate monohydrate was determined by elementary analysis. It gave positive ninhydrin, Rydon-Smith, and Hanes reactions. On high-voltage, paper electrophoresis under 3.5 kV for 15 minutes with 1 3 36 (v/v) formic acid-acetic add-water, the inactivated butirosin A moved 14.6 cm towards the cathode, whereas butirosin A moved 19.0 cm. It showed only end absorption in its u.v. spectrum, and a band at 960 cm (phosphoric ester) in the ij. spectrum. Hydrolysis by alkaline phosphatase yielded butirosin A. 

The n.m.r. spectrum of the inactivated butirosin A in deuterium oxide, with tetramethylsilane as the external reference standard (8 = 0), showed signals of the 4-amino-2-hydroxybutyryl moiety at 8 4.78 (/ 4.0 and 7.5 Hz, quartet, a-methine), 3.63 (/ 7.5 Hz, triplet, y-methylene) and -- 2.5 (multiplet, /3-methylene). The chemical shifts of these signals were the... 

The inactivated butirosin A moves toward the cathode 14.6 cm, while butirosin A moves 19.0 cm Ref. 

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