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• W1772521583 abstract "Class II Aminoacyl-tRNA synthetases are a set of very ancient multi domain proteins. The evolution of the catalytic domain of Class II synthetases can be reconstructed from three peptidyl-hairpins. Further evolution from this primordial catalytic core leads to a split of the Class II synthetases into two divisions potentially associated with the operational code. The earliest form of this code likely coded predominantly Glycine (Gly), Proline (Pro), Alanine (Ala) and Lysine/Aspartic acid (Lys/Asp). There is a paradox in these synthetases beginning with a hairpin structure before the Genetic Code existed. A resolution is found in the suggestion that the primordial Aminoacyl synthetases formed in a transition from a Thioester world to a Phosphate ester world." @default.
• W1772521583 created "2016-06-24" @default.
• W1772521583 creator A5058107013 @default.
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• W1772521583 date "2015-10-20" @default.
• W1772521583 modified "2023-10-10" @default.
• W1772521583 title "The evolution of Class II Aminoacyl-tRNA synthetases and the first code" @default.
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• W1772521583 doi "https://doi.org/10.1016/j.febslet.2015.10.006" @default.
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