ArticleAntimicrobial agents and chemotherapy2012
Cosubstrate tolerance of the aminoglycoside resistance enzyme Eis from Mycobacterium tuberculosis.
Article in Antimicrobial agents and chemotherapy, 2012. 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, 20 citations in OpenAlex.
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Comparative Proteomic Analysis of Cell Wall Proteins of Aminoglycosides Resistant and SensitiveCurrent protein & peptide science · 2025Article
- Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other Roles.Frontiers in microbiology · 2019Article
- Niche partitioning of a pathogenic microbiome driven by chemical gradients.Science advances · 2018Article
- Potent 1,2,4-Triazino[5,6 b]indole-3-thioether Inhibitors of the Kanamycin Resistance Enzyme Eis from Mycobacterium tuberculosis.ACS infectious diseases · 2018Article
- Comprehensive review of chemical strategies for the preparation of new aminoglycosides and their biological activities.Chemical Society reviews · 2018Review
- Sulfonamide-Based Inhibitors of Aminoglycoside Acetyltransferase Eis Abolish Resistance to Kanamycin in Mycobacterium tuberculosis.Journal of medicinal chemistry · 2016Article
- Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis.ACS chemical biology · 2016Article
- Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives.MedChemComm · 2016Article
- Amphiphilic Tobramycin Analogues as Antibacterial and Antifungal Agents.Antimicrobial agents and chemotherapy · 2015Article
- Comparative Study of Eis-like Enzymes from Pathogenic and Nonpathogenic Bacteria.ACS infectious diseases · 2015Article
- Biochemical and structural analysis of an Eis family aminoglycoside acetyltransferase from bacillus anthracis.Biochemistry · 2015Article
- New trends in aminoglycosides use.MedChemComm · 2014Article
- Domain dissection and characterization of the aminoglycoside resistance enzyme ANT(3″)-Ii/AAC(6')-IId from Serratia marcescens.Biochimie · 2013Article
- Biochemical and structural analysis of aminoglycoside acetyltransferase Eis from Anabaena variabilis.Molecular bioSystems · 2012Article
- A review of patents (2011-2015) towards combating resistance to and toxicity of aminoglycosides.MedChemCommArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We previously demonstrated that aminoglycoside acetyltransferases (AACs) display expanded cosubstrate promiscuity. The enhanced intracellular survival (Eis) protein of Mycobacterium tuberculosis is responsible for the resistance of this pathogen to kanamycin A in a large fraction of clinical isolates. Recently, we discovered that Eis is a unique AAC capable of acetylating multiple amine groups on a large pool of aminoglycoside (AG) antibiotics, an unprecedented property among AAC enzymes. Here, we report a detailed study of the acyl-coenzyme A (CoA) cosubstrate profile of Eis. We show that, in contrast to other AACs, Eis efficiently uses only 3 out of 15 tested acyl-CoA derivatives to modify a variety of AGs. We establish that for almost all acyl-CoAs, the number of sites acylated by Eis is smaller than the number of sites acetylated. We demonstrate that the order of n-propionylation of the AG neamine by Eis is the same as the order of its acetylation. We also show that the 6' position is the first to be n-propionylated on amikacin and netilmicin. By sequential acylation reactions, we show that AGs can be acetylated after the maximum possible n-propionylation of their scaffolds by Eis. The information reported herein will advance our understanding of the multiacetylation mechanism of inactivation of AGs by Eis, which is responsible for M. tuberculosis resistance to some AGs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.