EC Number   |
General Information |
Reference |
|---|
    6.1.1.24 | evolution |
evolution in the GlxRS family, overview. Two pathways exist for the formation of Gln-tRNAGln. The evolutionarily older indirect route utilizes a non-discriminating glutamyl-tRNA synthetase, ND-GluRS, that can form both Glu-tRNAGlu and Glu-tRNAGln. The Glu-tRNAGln is then converted to Gln-tRNAGln by an amidotransferase. ND-GluRS is the evolutionary predecessor of both the glutaminyl-tRNA synthetase, GlnRS, and the eukaryotic discriminating GluRS |
716375 |
| 6.1.1.24 | evolution |
ND-GluRS is a class I aminoacyl-tRNA synthetase |
716371 |
| 6.1.1.24 | metabolism |
the malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln |
745335 |
| 6.1.1.24 | more |
a hybrid enzyme, in which 23 amino acids from the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase, GlnRS, are replaced with the corresponding residues of human glutamyl-tRNA synthetase, GluRS, synthesizes Glu-tRNAGln over 104fold more efficiently than GlnRS. Identification of residues involved in improving complementarity for glutamate and in communicating between amino acid and tRNA binding sites, overview |
714207 |
| 6.1.1.24 | more |
ND-GluRS:GatDE complex formation and structure, detailed overview |
716371 |
| 6.1.1.24 | physiological function |
for synthesis of Gln-tRNAGln, a two-step process is required: the non-discriminating glutamyl-tRNA synthetase, ND-GluRS, forms Glu-tRNAGln, while the heterodimeric amidotransferase GatDE converts this mischarged tRNA to Gln-tRNAGln. A similar complex for Gln-tRNAGln formation in Methanothermobacter thermautotrophicus that allows the mischarged Glu-tRNAGln made by the tRNA synthetase to be channeled to the amidotransferase. The association of archaeal ND-GluRS with GatDE sequesters the tRNA synthetase for Gln-tRNAGln formation, with GatDE reducing the affinity of ND-GluRS for tRNAGlu by at least 13fold. The archaeal complex does not require tRNA for its formation, is not stable through product (Gln-tRNAGln) formation, and has no major effect on the kinetics of tRNAGln glutamylation nor transamidation |
716371 |
| 6.1.1.24 | physiological function |
ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGln by Glu-tRNAGln amidotransferase. GluRS avoids competition with Glu-tRNAGln amidotransferase GatCAB and glutamylates tRNAGln |
713616 |
| 6.1.1.24 | physiological function |
Plasmodium apicoplast protein synthesis is essential for parasite survival, aminoacyl-tRNA formation is essential for protein synthesis. The malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln. Formation of apicoplast Gln-tRNAGln proceeds via indirect aminoacylation. The nucleus-encoded non-discriminating GluRS is imported into the apicoplast is responsible for the formation of misacylated Glu-tRNAGln and is essential in the erythrocytic stages |
745335 |
