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Journal of Antimicrobial Chemotherapy (1987) 20, 803-813
© 1987 The British Society for Antimicrobial Chemotherapy

research-article

AAC(1): a new aminoglycoside-acetylating enzyme modifying the Cl aminogroup of apramycin

A.M. Lovering, L.O. White and D.S. Reeves

Department of Medical Microbiology, Southmead Hospital Bristol, U.K.

accepted 29 July 1987

An aminoglycoside-acetylating enzyme produced by a strain of Escherichia coli with an unusual resistance phenotype was characterized. This enzyme was found to mono-acetylate apramycin, butirosin, lividomycin and paromomycin and di-acetylate ribostamycin and neomycin to give reaction products which were distinguishable by HPLC analysis from those of AAC(2'), AAC(3) and AAC(6') enzymes. The enzyme, however, was not found to acetylate amikacin, fortimicin, geneticin, gentamicin, kanamycin A, netilmicin or tobramycin. The reaction product from the action of this enzyme on apramycin was purified and identified by nuclear magnetic resonance studies as 1-N-acetyl apramycin. The second site at which ribostamycin and neomycin B were modified by this enzyme was not determined but is postulated as the 6'-amino group. It is proposed that this enzyme be named AAC(1).


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