6.1.1.17 ATP + L-glutamate + tRNAGln - 6.1.1.17 ATP + L-glutamate + tRNAGln enzyme expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli 6.1.1.17 ATP + L-glutamate + tRNAGln isozyme 2 expressed in an Escherichia coli mutant strain, tRNAGln UUG from Escherichia coli 6.1.1.17 ATP + L-glutamate + tRNAGln(CUG) the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG) 6.1.1.17 ATP + L-glutamate + tRNAGln(UUG) the enzyme shows a significant catalytic preference for tRNAGln(CUG) compared to the less active tRNAGln(UUG) 6.1.1.17 ATP + L-glutamate + tRNAGlu - 6.1.1.17 ATP + L-glutamate + tRNAGlu isozyme 1 expressed in an Escherichia coli mutant strain, tRNAGlu from Escherichia coli 6.1.1.17 ATP + L-glutamate + tRNAGlu recombinant mutant Q373R expressed in Escherichia coli mutant strain, tRNAGlu from Escherichia coli 6.1.1.17 ATP + L-glutamate + tRNAGlu eukaryotic-type discriminating glutamyl-tRNA synthetase, inability to utilize Escherichia coli tRNA as substrate. The enzyme is essential for growth of insect stage Trypanosoma brucei and is responsible for essentially all of the glutamyl-tRNA synthetase activity in cytosol and in mitochondria 6.1.1.17 ATP + L-glutamate + tRNAGlu glutamyl-tRNA, formed by Glu-tRNA synthetase, is a substrate for protein biosynthesis and tetrapyrrole formation by the C5 pathway 6.1.1.17 ATP + L-glutamate + tRNAGlu wild-type enzyme and chimeric mutant cGluGlnRS, overview 6.1.1.17 ATP + L-glutamate + tRNAGlu involved in synthesis of 5-aminolevulinate (a committed and regulated precursor in the chlorophyll biosynthetic pathway) 6.1.1.17 additional information no charging of Escherichia coli tRNAGln by enzyme mutant Q373R 6.1.1.17 additional information the recombinant wild-type enzyme is toxic for Escherichia coli, probably due to its charging of both tRNAGlu and tRNAGln 6.1.1.17 additional information GluRS plays a major role in regulating the cellular level of heme, aminoacylation of tRNAGlu correlates with the demand of heme, a transcriptional mechanism might control the level of GluRS1 in cells grown in Fe2+, under growth conditions in which cells do not require Glu-tRNA, as precursor for heme biosynthesis, up to 85% of GluRS1 is dispensable, but no major detrimental effect in the cell growth is observed. Thus, GluRS2 and the remaining 15% of the activity of GluRS1 are sufficient to provide the Glu-tRNA substrates for protein synthesis 6.1.1.17 additional information GtS is an age-dependent Streptococcus pneumoniae antigen and is a surface-located adhesin that is capable of inducing a partially protective immune response against Streptococcus pneumoniae in mice, overview 6.1.1.17 additional information regulation of gltX expression, overview, the gene glxT encoding the enzyme is involved in regulation of other genes's expression, mechanisms, overview 6.1.1.17 additional information the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression