• DOI:10.7164/ANTIBIOTICS.51.735
Corpus ID: 30391035

The novel enzymatic 3''-N-acetylation of arbekacin by an aminoglycoside 3-N-acetyltransferase of Streptomyces origin and the resulting activity.

@article{Hotta1998TheNE,
  title={The novel enzymatic 3''-N-acetylation of arbekacin by an aminoglycoside 3-N-acetyltransferase of Streptomyces origin and the resulting activity.},
  author={K. Hotta and A. Sunada and J. Ishikawa and S. Mizuno and Y. Ikeda and S. Kondo},
  journal={The Journal of antibiotics},
  year={1998},
  volume={51 8},
  pages={
          735-42
        }
}

• K. Hotta, A. Sunada, +3 authors S. Kondo
• Published 1998
• Biology, Medicine
• The Journal of antibiotics

Kanamycin group antibiotics were subjected to enzymatic acetylation by a cell free extract containing an aminoglycoside 3-N-acetyltransferase, AAC(3)-X, derived from Streptomyces griseus SS-1198PR. Characterization of the incubated reaction mixtures by TLC and antibiotic assay revealed that a product retaining activity was specifically formed from arbekacin, an anti-MRSA semisynthetic aminoglycoside. The structural determination demonstrated that acetylation occurred at the 3"-amino group in… Expand

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