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Appl Environ Microbiol. 1968 September; 16(9): 1276-1281
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Inactivation of Kanamycin, Neomycin, and Streptomycin by Enzymes Obtained in Cells of Pseudomonas aeruginosa

Institute of Applied Microbiology, University of Tokyo, Tokyo, Japan

ABSTRACT

Ten strains of Pseudomonas aeruginosa were disrupted and centrifuged. The supernatant fluids from centrifugation at 105,000 x g contained enzymes inactivating kanamycin, neomycin, and streptomycin in the presence of adenosine triphosphate. Kanamycin-inactivating enzyme was precipitated with ammonium sulfate at 66% of saturated concentration, and the inactivated kanamycin was shown to be kanamycin-3'-phosphate in which the C-3 hydroxyl group of 6-amino-6-deoxy-D-glucose moiety was phosphorylated. This is identical with kanamycin inactivated by Escherichia coli carrying R factor. Streptomycin-inactivating enzyme was precipitated with ammonium sulfate at 33% of saturated concentration.