ArticleAntimicrobial agents and chemotherapy2013
Novel aminoglycoside 2''-phosphotransferase identified in a gram-negative pathogen.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- First molecular characterization and antimicrobial resistance profiles of Campylobacter jejuni isolated from poultry meat in Yemen.Scientific reports · 2026Article
- Antibiotic Resistance inAntibiotics (Basel, Switzerland) · 2023Review
- Identification and characterization of a novel chromosomal aminoglycoside 3'-Frontiers in microbiology · 2023Article
- Aminoglycoside Resistance and Possible Mechanisms inFrontiers in microbiology · 2021Article
- Gene pool transmission of multidrug resistance among Campylobacter from livestock, sewage and human disease.Environmental microbiology · 2019Article
- Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2''-phosphotransferases.Acta crystallographica. Section D, Structural biology · 2019Article
- Whole-Genome Sequence Analysis of Multidrug-Resistant Campylobacter Isolates: a Focus on Aminoglycoside Resistance Determinants.Journal of clinical microbiology · 2018Article
- Nucleoside triphosphate cosubstrates control the substrate profile and efficiency of aminoglycoside 3'-MedChemComm · 2018Article
- Review
- Antimicrobial Resistance inMicrobiology spectrum · 2018Review
- Cloning and Expression of Novel Aminoglycoside Phosphotransferase Genes from Campylobacter and Their Role in the Resistance to Six Aminoglycosides.Antimicrobial agents and chemotherapy · 2018Article
- Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im.Microbial cell (Graz, Austria) · 2017Article
- High Prevalence and Predominance of theAntimicrobial agents and chemotherapy · 2017Article
- Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives.MedChemComm · 2016Article
- Novel gentamicin resistance genes in Campylobacter isolated from humans and retail meats in the USA.The Journal of antimicrobial chemotherapy · 2015Article
- Whole-genome sequencing of gentamicin-resistant Campylobacter coli isolated from U.S. retail meats reveals novel plasmid-mediated aminoglycoside resistance genes.Antimicrobial agents and chemotherapy · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Aminoglycoside 2″-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci. We describe a novel aminoglycoside 2″-phosphotransferase from the Gram-negative pathogen Campylobacter jejuni, which shares 78% amino acid sequence identity with the APH(2″)-Ia domain of the bifunctional aminoglycoside-modifying enzyme aminoglycoside (6') acetyltransferase-Ie/aminoglycoside 2″-phosphotransferase-Ia or AAC(6')-Ie/APH(2″)-Ia from Gram-positive cocci, which we called APH(2″)-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin, but not to any of the 4,5-disubstituted antibiotics tested. Steady-state kinetic studies demonstrated that GTP, and not ATP, is the preferred cosubstrate for APH(2″)-If. The enzyme phosphorylates the majority of 4,6-disubstituted aminoglycosides with high catalytic efficiencies (k(cat)/K(m) = 10(5) to 10(7) M(-1) s(-1)), while the catalytic efficiencies against the 4,6-disubstituted antibiotics amikacin and isepamicin are 1 to 2 orders of magnitude lower, due mainly to the low apparent affinities of these substrates for the enzyme. Both 4,5-disubstituted antibiotics and the atypical aminoglycoside neamine are not substrates of APH(2″)-If, but are inhibitors. The antibiotic susceptibility and substrate profiles of APH(2″)-If are very similar to those of the APH(2″)-Ia phosphotransferase domain of the bifunctional AAC(6')-Ie/APH(2″)-Ia enzyme.
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