Substrate Specificity and Catalysis by the Editing Active Site of Alanyl-tRNA Synthetase from Escherichia coli
Author:
Affiliation:
1. Department of Biochemistry, College of Medicine, Health Sciences Complex, 89 Beaumont Avenue, University of Vermont, Burlington, Vermont 05405, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1013535
Reference56 articles.
1. Fidelity at the Molecular Level: Lessons from Protein Synthesis
2. A sequence element that tunes Escherichia coli tRNAAlaGGC to ensure accurate decoding
3. Bases in the anticodon loop of tRNAAlaGGC prevent misreading
4. Editing of errors in selection of amino acids for protein synthesis
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1. Coordination between aminoacylation and editing to protect against proteotoxicity;Nucleic Acids Research;2023-09-23
2. Design principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis;Nucleic Acids Research;2023-03-23
3. Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases;Nucleic Acids Research;2022-03-31
4. Escherichia coli alanyl-tRNA synthetase maintains proofreading activity and translational accuracy under oxidative stress;Journal of Biological Chemistry;2022-03
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