By Sunghoon Kim
This publication will specialise in new molecular interactions and novel actions and the linked illnesses which have been lately came across from the stories of eukaryotic and mammalian aminoacyl-tRNA synthetases. moreover, the aptitude purposes of ARS researches in biotechnology and medication could be addressed.
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Extra info for Aminoacyl-tRNA Synthetases in Biology and Medicine
The finding that product release is rate-limiting for class I editing enzymes, and that class II enzymes are instead rate-limited by an early step in the pathway, helps to rationalize why trans editing generally does not occur in class I systems [46, 97, 159]. However, TyrRS can misacylate tRNATyr with D-tyrosine [218–220], and the D-Tyr-tRNATyr deacylase functions as a trans editing protein to clear this species. Interestingly, this enzyme is structurally related to the editing domain of archaeal ThrRS, which hydrolyzes Ser-tRNAThr either as a component of the full-length ThrRS or as a free-standing protein [199, 214].
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RNA 18:213–221 96. Mulvey RS, Fersht AR (1978) Mechanism of aminoacylation of transfer RNA. A pre-steadystate analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilus. Biochemistry 17:5591–5597 97. Cvetesic N, Perona JJ, Gruic-Sovulj I (2012) Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and posttransfer hydrolytic steps. J Biol Chem 287:25381–25394 98. Ward WH, Fersht AR (1988) Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA.
Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim