Literature DB >> 26270859

A Novel 6'-N-Aminoglycoside Acetyltransferase, AAC(6')-Ial, from a Clinical Isolate of Serratia marcescens.

Tatsuya Tada1, Tohru Miyoshi-Akiyama2, Kayo Shimada1, Rajan K Dahal3, Shyam K Mishra3, Hiroshi Ohara4, Teruo Kirikae1, Bharat M Pokhrel3.   

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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Year:  2015        PMID: 26270859     DOI: 10.1089/mdr.2015.0126

Source DB:  PubMed          Journal:  Microb Drug Resist        ISSN: 1076-6294            Impact factor:   3.431


  2 in total

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Authors:  Maria S Ramirez; Marcelo E Tolmasky
Journal:  Molecules       Date:  2017-12-19       Impact factor: 4.411

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  2 in total

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