Abstract
Serratia marcescens IOMTU115 has a novel 6′-N-aminoglycoside acetyltransferase-encoding gene, aac(6′)-Ial. The encoded protein AAC(6′)-Ial has 146 amino acids, with 91.8% identity to the amino acid sequence of AAC(6′)-Ic in S. marcescens SM16 and 97.3% identity to the amino acid sequence of AAC(6′)-Iap in S. marcescens WW4. The minimum inhibitory concentrations of aminoglycosides for Escherichia coli expressing AAC(6′)-Ial were similar to those for E. coli expressing AAC(6′)-Ic or AAC(6′)-Iap. Thin-layer chromatography showed that AAC(6′)-Ial, AAC(6′)-Ic, or AAC(6′)-Iap acetylated all the aminoglycosides tested, except for apramycin, gentamicin, and lividomycin. Kinetics assays revealed that AAC(6′)-Ial is a functional acetyltransferase against aminoglycosides. The aac(6′)-Ial gene was located on chromosomal DNA.
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