ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2019
Antibiotic resistance and inhibition mechanism of novel aminoglycoside phosphotransferase APH(5) from B. subtilis subsp. subtilis strain RK.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- Targeting bacterial kinases as a strategy to counteract antibiotic resistance.Communications chemistry · 2025Article
- Integrated Genomic and Phenotypic Analysis ofMicroorganisms · 2025Article
- Antibiotic Resistance Gene Expression in Veterinary Probiotics: Two Sides of the Coin.Veterinary sciences · 2025Review
- Restoring susceptibility to aminoglycosides: identifying small molecule inhibitors of enzymatic inactivation.RSC medicinal chemistry · 2023Review
- Prevalence of Antimicrobial Resistance and Respective Genes amongInternational journal of environmental research and public health · 2022Article
- Purification and characterization of antibacterial surfactin isoforms produced by Bacillus velezensis SK.AMB Express · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Bacterial resistance towards aminoglycoside antibiotics mainly occurs because of aminoglycoside phosphotransferases (APHs). It is thus necessary to provide a rationale for focusing inhibitor development against APHs. The nucleotide triphosphate (NTP) binding site of eukaryotic protein kinases (ePKs) is structurally conserved with APHs. However, ePK inhibitors cannot be used against APHs due to cross reactivity. Thus, understanding bacterial resistance at the atomic level could be useful to design new inhibitors against such resistant pathogens. Hence, we carried out in vitro studies of APH from newly deposited multidrug-resistant organism Bacillus subtilis subsp. subtilis strain RK. Enzymatic modification studies of different aminoglycoside antibiotics along with purification and characterization revealed a novel class of APH, i.e., APH(5), with molecular weight 27 kDa approximately. Biochemical analysis of virtually screened inhibitor ZINC71575479 by coupled spectrophotometric assay showed complete enzymatic inhibition of purified APH(5). In silico toxicity study comparison of ZINC71575479 with known inhibitor of APH, i.e., tyrphostin AG1478, predicted its acceptable values for 96 h fathead minnow LC
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