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Ten strains ofPseudomonas aeruginosa were disrupted and centrifuged. The supernatant fluids from centrifugation at 105,000 ×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 byEscherichia coli carrying R factor. Streptomycin-inactivating enzyme was precipitated with ammonium sulfate at 33% of saturated concentration.

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