EC Number   |
Natural Substrates |
|---|
    6.1.1.19 | ATP + L-arginine + tRNAArg |
- |
| 6.1.1.19 | ATP + L-arginine + tRNAArg |
the C-terminal extension of the human cytosolic leucyl-tRNA synthetase is indispensable for its interaction with the N-terminal of human cytosolic arginyl-tRNA synthetase in the macromolecular complex |
| 6.1.1.19 | ATP + L-arginine + tRNAArg |
L-arginine is the best substrate |
| 6.1.1.19 | ATP + L-arginine + tRNAArg |
the complexed enzyme supplies arginyl-tRNA for the protein synthesis |
| 6.1.1.19 | more |
the free enzyme provides arginyl-tRNA for the NH2-terminal arginine modification of proteins by arginyl-tRNA:protein arginyltransferase, EC 2.3.2.8 |
| 6.1.1.19 | more |
key role in protein synthesis as part of a multienzyme complex |
| 6.1.1.19 | more |
arginyl-tRNA synthetase, MtArgRS, directly and stably interacts with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C |
