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Issue 36, 2013
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Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

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Abstract

Aminoacyl-tRNAs serve as amino acid donors in many reactions in addition to protein synthesis by the ribosome, including synthesis of the peptidoglycan network in the cell wall of bacterial pathogens. Synthesis of analogs of aminoacylated tRNAs is critical to further improve the mechanism of these reactions. Here we have described the synthesis of two non-isomerizable analogues of Ala-tRNAAla containing an amide bond instead of the isomerizable ester that connects the amino acid with the terminal adenosine in the natural substrate. The non-isomerizable 2′ and 3′ regioisomers were not used as substrates by FemXWv, an alanyl-transferase essential for peptidoglycan synthesis, but inhibited this enzyme with IC50 of 5.8 and 5.5 μM, respectively.

Graphical abstract: Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

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Publication details

The article was received on 11 Jun 2013, accepted on 22 Jul 2013 and first published on 08 Aug 2013


Article type: Paper
DOI: 10.1039/C3OB41206G
Org. Biomol. Chem., 2013,11, 6161-6169

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    Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

    D. Mellal, M. Fonvielle, M. Santarem, M. Chemama, Y. Schneider, L. Iannazzo, E. Braud, M. Arthur and M. Etheve-Quelquejeu, Org. Biomol. Chem., 2013, 11, 6161
    DOI: 10.1039/C3OB41206G

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