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Results 1 - 10 of 17 > >>
EC Number General Information Commentary Reference
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17evolution many bacterial GluRS are capable of recognizing two tRNA substrates: tRNAGlu and tRNAGln, e.g. GluRS from such as Bacillus subtilis, Thermosynechococcus elongatus, and Mycobacterium tuberculosis. In bacteria such as Escherichia coli and Thermus thermophilus that possess glutaminyl-tRNA synthetase (GlnRS), the cognate aminoacylating enzyme for tRNAGln, GluRS exclusively glutamylates tRNAGlu. tRNA-GluRS interaction in bacteria is also associated with phylum-specific idiosyncrasies, structure-function analysis, overview 743955
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17evolution the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme -, 745552
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17evolution the structures of the active sites of bacterial and mammalian GluRSs differ significantly 746179
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17evolution the tRNA binding site is less conserved than either the Glu or the ATP binding site. Certain amino acids, including Arg147, which interacts with the tRNAGlu C74 phosphate, and Asp44 and Arg47, which interact with the 2'-hydroxyl group of C75, as well as Tyr187 and Thr43, which interact with the adenosine base and the 5'-hydroxyl group of A76, are strictly conserved -, 745395
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17malfunction EPRS-haploid (Eprs+/-) mice show enhanced viremia and inflammation and delayed viral clearance 745867
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17metabolism the sensitivity to oxidation of GluRS1 might provide a means to regulate tetrapyrrole and protein biosynthesis in response to extreme changes in both the redox and heme status of the cell via a single enzyme. The glutamate moiety of Glu-tRNAGlu is transformed to glutamate semialdehyde by the glutamyl-tRNA reductase and is subsequently transformed to 4-aminolevulinic acid, the universal precursor of tetrapyrroles, by the glutamate semialdehyde amidotransferase 714031
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17metabolism under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview 745867
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17more analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview -, 745552
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17more homology structure modeling using structures of GluRSs identified from Burkholderia thailandensis and Thermosynechococcus elongatus, Uniprot IDs Q2SX36 and Q8DLI5, respectively, as search template, molecular docking 746179
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17more targets for oxidation-based inhibition are cysteines from a SWIM zinc-binding motif located in the tRNA acceptor helix-binding domain. Oxidation of the metal-binding site cysteine of GluRS1 significantly impaired catalysis. Also, binding of ATP or tRNA protects the distant cysteines of the SWIM motif 714031
Results 1 - 10 of 17 > >>