EC Number   |
General Information |
Reference |
|---|
    6.1.1.16 | evolution |
although the nucleotides in tRNA required for aminoacylation are conserved in evolution, bacterial aminoacyl-transfer RNA synthetases are unable to acylate eukaryote-specific tRNA. Whereas Escherichia coli CysRS cannot acylate human tRNACys, the fusion of a eukaryote-specific domain of human CysRS overcomes the cross-species barrier in human tRNACys. In addition to enabling recognition of the sequence differences in the tertiary core of tRNACys, the fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals. The accuracy of codon recognition on the ribosome is also highly sensitive to the A37G transition in tRNACys |
716319 |
| 6.1.1.16 | evolution |
multiple genes encode for aminoacyl-tRNA synthetases from Mycobacterium smegmatis, e.g. glutamyl (GluRS), cysteinyl (CysRS), prolyl (ProRS) and lysyl (LysRS) tRNA synthetases |
-, 746197 |
| 6.1.1.16 | malfunction |
mutations in isoform CARS2 result in a mitochondrial translational defect leading to mitochondrial epileptic encephalopathy |
745531 |
| 6.1.1.16 | metabolism |
the enzyme plays a crucial role in endogenous cysteine hydropersulfide production and serves as the principal cysteine persulfide synthase in vivo |
745862 |
| 6.1.1.16 | physiological function |
Essentiality of lysyl and cysteinyl-tRNA synthetases of Mycobacterium smegmatis |
-, 746197 |
| 6.1.1.16 | physiological function |
the enzyme is essential for growth |
746197 |
