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. 1975 Nov;28(11):845-53.
doi: 10.7164/antibiotics.28.845.

Aminoglycoside 3'-phosphotransferase III, a new phosphotransferase. Resistance mechanism

Free article

Aminoglycoside 3'-phosphotransferase III, a new phosphotransferase. Resistance mechanism

Y Umezawa et al. J Antibiot (Tokyo). 1975 Nov.
Free article

Abstract

The aminoglycoside phosphotransferase of Pseudomonas aeruginosa 21-75 was purified by affinity chromatography using dibekacin-Sephadex 4B or lividomycin A-Sepharose 4B followed by DEAE Sephadex A-50 chromatography. It had activities of both the known aminoglycoside 3'-phosphotransferases I and II, and transferred phosphate from ATP to the 3'-hydroxyl group of kanamycin A, ribostamycin and butirosin A and 5-hydroxyl group of lividomycin A. This enzyme was designated aminoglycoside 3'-phosphotransferase III. It showed strong substrate inhibition by kanamycin A and ribostamycin when their concentration exceeded 6 muM. Purification and characterization of this enzyme are reported.

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