Kinetic Constants of Activation and Misactivation by LeutRNASynthetase

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Organism Bacteria Escherichia coli
Reference Chen JF, Guo NN, Li T, Wang ED, Wang YL. CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function. Biochemistry. 2000 Jun 6 39(22):6726-31.PubMed ID10828991
Method Construction of a Plasmid Containing the Gene Encoding His6-Tagged LeuRS-B. Cloning and Expression of the Gene Encoding CP1Leu. Assay of Enzyme ActiVity. Circular Dichroism (CD) Spectroscopy.
Comments Aminoacyl-tRNA synthetases (aaRSs)1 arose early in evolution and are believed to be a group of ancient enzymes that catalyze the precise charging of tRNAs with their cognate amino acids (1). The aminoacylation of tRNA is a two-step reaction: (a) activation of amino acids with ATP by forming aminoacyl adenylates and (b) transferring of the aminoacyl residue from the aminoacyl adenylate to the cognate tRNA substrate (2). The accuracy of aminoacylation depends on both the specific recognition of amino acids during their activations (coarse sieve) and the pre- or posttransferring editing (fine sieve) that correct errors at either the aminoacyl adenylate level or the tRNA level.
Entered by Uri M
ID 104980