Translational incorporation of modified phenylalanines and tyrosines during cell-free protein synthesis (original) (raw)
* Corresponding authors
a Key Laboratory of Biocatalysis & Chiral Drug Synthesis of Guizhou Province, Generic Drug Research Center of Guizhou Province, School of Pharmacy, Zunyi Medical University, Zunyi, China
E-mail: zqwang@zmu.edu.cn
b Key Laboratory of Basic Pharmacology of Ministry of Education and Joint International Research Laboratory of Ethnomedicine of Ministry of Education, Zunyi Medical University, Zunyi, China
c Research School of Chemistry, Australian National University, 137 Sullivans Creek Road, Acton ACT 2601, Australia
d Australian National University Medical School, 54 Mills Road, Acton ACT 2601, Australia
E-mail: Hayden.Matthews@anu.edu.au
Abstract
Inherent promiscuity of bacterial translation is demonstrated by mass spectrometric quantification of the translational incorporation of ring-substituted phenylalanines and tyrosines bearing fluoro-, hydroxyl-, methyl-, chloro- and nitro-groups in an _E. coli_-derived cell-free system. Competitive studies using the cell-free system show that the aminoacyl-tRNA synthetases (aaRS) have at least two orders of magnitude higher specificity for the native substrate over these structural analogues, which correlates with studies on the purified synthetase.
- This article is part of the themed collection:Editors' Collection: Fluorine chemistry in medicinal chemistry and chemical biology
This article is Open Access
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