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Inactivation of Kanamycin A by Phosphorylation in Pathogenic Nocardia
Author(s) -
Yazawa Katsukiyo,
Mikami Yuzuru,
Maeda Akio,
Kudo Takuji,
Suzuki Kenichiro,
Saito Naoki,
Kubo Akinori
Publication year - 1991
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1991.tb01531.x
Subject(s) - kanamycin , aminoglycoside , biology , microbiology and biotechnology , nocardia , antibiotics , actinomycetales , bacteria , streptomyces , genetics
Among the five species of pathogenic Nocardia , i.e., N. asteroides, N. brasiliensis, N. farcinica, N. nova and N. otitidiscaviarum , all strains of N. brasiliensis and N. farcinica showed resistance to an aminoglycoside antibiotic, kanamycin A, showing the MIC (minimum inhibitory concentration) values of more than 100 μg/ml. This species‐specific difference in sensitivity was found to be explained by the production of an inactivation enzyme, aminoglycoside 3′‐phosphotransferase APH(3′). Structural studies by mass and NMR spectroscopy on the inactivated substance produced by a cell‐free extract of the Nocardia confirmed the conversion of kanamycin A to an inactive substance, kanamycin A 3′‐phosphate. The MIC values of N. otitidiscaviarum and N. nova for kanamycin A, on the other hand, ranged from 0.78 μg/ml to 100 μg/ml, and both species were non‐producers of APH(3′). Sensitivity to the antibiotic and APH(3′) productivity of N. asteroides varied depending on the strain.