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New PDF release: Aminoacyl-tRNA Synthetases in Biology and Medicine

By Sunghoon Kim

ISBN-10: 940178700X

ISBN-13: 9789401787000

ISBN-10: 9401787018

ISBN-13: 9789401787017

This e-book will concentrate on 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. furthermore, the capability purposes of ARS researches in biotechnology and drugs should be addressed.

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Extra resources for Aminoacyl-tRNA Synthetases in Biology and Medicine

Sample text

Studies on class II aaRS are consistent with the kinetic partitioning model and with the notion that pre-transfer editing is a synthetic site activity. In ThrRS, pre-transfer editing was enhanced in a designed mutant with a lowered rate of aminoacyl transfer, providing an independent observation that the rates of these reactions are inversely related [161]. ThrRS and ProRS exhibit robust pre-transfer editing of serine and alanine, respectively, in the absence of tRNA, and enzyme homologs in both systems that naturally lack editing domains are also capable of this activity [161, 162, 179, 180].

J Mol Biol 362:1159–1180 82. Retailleau P, Weinreb V, Hu M, Carter CW Jr (2007) Crystal structure of tryptophanyl-tRNA synthetase complexed with adenosine-50 tetraphosphate: evidence for distributed use of catalytic binding energy in amino acid activation by class I aminoacyl-tRNA synthetases. J Mol Biol 369:108–128 83. Laowanapiban P, Kapustina M, Vonrhein C, Delarue M, Koehl P, Carter CW Jr (2009) Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.

B) Structure of a portion of the post-transfer editing domain of class II ThrRS bound to the post-transfer editing substrate analog serine 30 -aminoadenosine (PDB code 1TKY). (c) Schematic description of the proposed stereochemical mechanism of post-transfer editing hydrolysis in ThrRS, based on the crystal structure depicted in panel (b) the nucleophilic water molecule, and a lysine residue participates in water-mediated stabilization of the departing O30 anion. The mechanism is corroborated by sharp decreases measured in the catalytic rate upon mutation of either of these amino acids [212].

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Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim

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