Evidence for single mechanism for aminoacyl-tRNA synthetases including aminoacyl adenylates as intermediates.

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Evidence for single mechanism for aminoacyl-tRNA synthetases including aminoacyl adenylates as intermediates.

The rate of transfer of amino acid from enzyme-bound aminoacyl adenylate to tRNA has been compared with the rate of esterification of free amino acid. The approach of Lövgren et al. (Lövgren, T. N. E., Heinonen, J., and Loftfield, R. B. (1975) J. Biol. Chem. 250, 3854-3860) was used, with 14C in the aminoacyl adenylate and 3H in the free amino acid and with both the lysine and isoleucine system...

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Aminoacyl-tRNA synthetases database

Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the firs...

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Acetylation regulates aminoacyl-tRNA synthetases

Previous proteomic analyses have shown that aminoacyl-tRNA synthetases (aaRSs) in many organisms can be modified by acetylation of lysine (Lys). In this present study, leucyl-tRNA synthetase and arginyl-tRNA synthetase from Escherichia coli (EcLeuRS and EcArgRS) were overexpressed and purified, and found to be acetylated on Lys residues by mass spectrometry (MS). Glutamine (Gln) scanning mutage...

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Aminoacyl-tRNA synthetases database Y2K

The aminoacyl-tRNA synthetases (AARS) are a diverse group of enzymes that ensure the fidelity of transfer of genetic information from DNA into protein. They catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. Currently, 818 AARS primary structures ha...

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Aminoacyl-tRNA Synthetases and Self-acylating Ribozymes

The aminoacyl-tRNA synthetases (aaRS) are at the heart of modern translation, catalyzing the accurate biosynthesis of aminoacyl-tRNAs (aa-tRNAs), the immediate precursors for encoded peptides. However, the first catalysts that made aa-RNAs for coded protein synthesis probably appeared long before any protein aaRS, to serve a preexisting translation system (see below). It presently seems likely ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1977

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)40515-1