Read e-book online Aminoacyl-tRNA Synthetases in Biology and Medicine PDF

By Sunghoon Kim

ISBN-10: 940178700X

ISBN-13: 9789401787000

ISBN-10: 9401787018

ISBN-13: 9789401787017

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

Example text

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].

Banik SD, Nandi N (2012) Mechanism of the activation step of the aminoacylation reaction: a significant difference between class I and class II synthetases. J Biomol Struct Dyn 30:701–715 52. Ibba M, Losey HC, Kawarabayasi Y, Kikuchi H, Bunjun S, Soll D (1999) Substrate recognition by class I lysyl-tRNA synthetases: a molecular basis for gene displacement. Proc Natl Acad Sci USA 96:418–423 53. Kern D, Lapointe J (1979) Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Study of the interactions with its substrates.

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.

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Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim


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