jbc.M112.372151.
30 Oct 2007 Aminoacyl-tRNA synthetases, a group of enzymes catalyzing aminoacyl-tRNA formation, may possess inherent editing activity to clear mistakes arising through the selection of non-cognate amino acid. It is generally assumed that both editing substrates, non-cognate aminoacyl-adenylate and misacylated
1 Aug 2000 A single cysteine residue (C443) that is located within the class II-specific motif 3 consensus sequence was shown previously to be dispensable for proline-tRNA synthetase aminoacylation activity. We show here that C443 is critical for the hydrolytic editing of Ala-tRNAPro by this class II synthetase.
Hydrolytic nucleoside and nucleotide deamination, and genetic instability: a possible link between RNA-editing enzymes and cancer? Shrikant Anant1 and Nicholas O. Davidson2. 1Department of Internal Medicine, Washington University School of Medicine, Saint Louis, MO 63110, USA. 2Departments of Internal Medicine,
from the mischarged tRNA by a hydrolytic editing mechanism before dissociation from the synthetase. Discrimination between cognate and non-cognate. tRNA by aminoacyl-tRNA synthetases is generally not so great as that observed for the amino acid sub- strate. Equilibrium binding studies and steady state. Km-values
Hydrolytic editing by a class II aminoacyl-. tRNA synthetase. Penny J. Beuning and Karin Musier-Forsyth. Department of Chemistry, University of Minnesota, 207 Pleasant Street Southeast, Minneapolis, MN 55455. Edited by Paul R. Schimmel, The Scripps Research Institute, La Jolla, CA, and approved June 8, 2000
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14 Mar 2008 In the absence of tRNA, enzyme-catalyzed Ala-AMP hydrolysis is the dominant form of editing, with “selective release" of noncognate adenylate from the active site constituting a minor pathway. Studies with human and Methanococcus jannaschii ProRS, which lack a post-transfer editing domain, suggest

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February 2018