Evidence map›Paper›PMID 42829885›Full record

ArticleBiotechnology letters2026

Inhibitors of Mycobacterium tuberculosis methionyl-tRNA synthetase are sensitive to the mutations E24A and L293A in aminoacyl-adenylate binding site.

Galyna P Volynets, Mariia O Usenko, Oksana B Gorbatiuk, Dmitry M Irodov, Sergiy S Lukashov, Volodymyr G Bdzhola, Svitlana V Antonenko, Svitlana V Marchenko, Sergiy S Tarnavskiy, Sergiy M Yarmoluk and 2 more

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Article in Biotechnology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

12 authors.

Galyna P VolynetsDepartment of Medicinal Chemistry, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine. g.p.volynets@gmail.com.
Mariia O UsenkoDepartment of Cell Regulatory Mechanisms, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Oksana B GorbatiukDepartment of Cell Regulatory Mechanisms, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Dmitry M IrodovDepartment of Cell Regulatory Mechanisms, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Sergiy S LukashovDepartment of Medicinal Chemistry, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Volodymyr G BdzholaDepartment of Medicinal Chemistry, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Svitlana V AntonenkoDepartment of Molecular Genetics, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Svitlana V MarchenkoDepartment of Biomolecular Electronics, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Sergiy S TarnavskiyDepartment of Medicinal Chemistry, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Sergiy M YarmolukDepartment of Medicinal Chemistry, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Oleksandra I SkydanovychDepartment of Protein Synthesis Enzymology, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.
Michael A TukaloDepartment of Protein Synthesis Enzymology, Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, 150 Zabolotnogo St., Kiev, 03143, Ukraine.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The objective of this study was to obtain Mycobacterium tuberculosis methionyl-tRNA synthetase (MetRS) mutant forms E24A and L293A and investigate the efficiency of M. tuberculosis MetRS inhibitors toward these mutant forms in order to predict binding mechanisms. The recombinant mutant M. tuberculosis MetRS E24A and L293A were obtained using overlap PCR. The recombinant proteins MetRS E24A and L293A were expressed in BL21(DE3) cells. The activity of obtained aminoacyl-tRNA synthetases was studied with aminoacylation assay using BIOMOL® Green Reagent. It was found that the mutations of Glu24 and Leu293 with alanine in the synthetic site of M. tuberculosis MetRS lead to significant decrease of inhibitory activity of investigated compounds. These findings suggest that the amino acid residues Glu24 and Leu293 may contribute to the inhibitory activity of the studied compounds and should therefore be considered during further structural optimization.

Indexed as

Adenosine MonophosphateEnzyme InhibitorsMethionine-tRNA LigaseMycobacterium tuberculosisBinding SitesEscherichia coliMutagenesis, Site-DirectedMutationRecombinant ProteinsAdenosine MonophosphateEnzyme InhibitorsMethionine-tRNA LigaseRecombinant ProteinsInhibitorMethionyl-tRNA synthetaseMycobacterium tuberculosisSite-directed mutagenesis

Identifiers

PMID42829885

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