Organism | UniProt | Comment | Textmining |
---|---|---|---|
Desulfitobacterium hafniense | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | molecular dynamics simulations of the structures of PylRS and its complexes with tRNAPyl and activated pyrrolysine, overview. Identification of key residues and interactions leading to shortest paths of communication in the structure networks of DhPylRS. Dimeric hPylRS in different states of ligation: Sys1 as native DhPylRS, Sys2 as DhPylRS-Pyl-AMP, and Sys3 as DhPylRS-Pyl-AMP-tRNA, detailed overview | Desulfitobacterium hafniense | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | molecular dynamics simulations of the structures of PylRS and its complexes with tRNAPyl and activated pyrrolysine, overview. Identification of key residues and interactions leading to shortest paths of communication in the structure networks of DhPylRS. Dmeric hPylRS in different states of ligation: Sys1 as native DhPylRS, Sys2 as DhPylRS-Pyl-AMP, and Sys3 as DhPylRS-Pyl-AMP-tRNA, detailed overview | Desulfitobacterium hafniense |
Synonyms | Comment | Organism |
---|---|---|
PylRS | - |
Desulfitobacterium hafniense |
pyrrolysyl-tRNA synthetase | - |
Desulfitobacterium hafniense |
General Information | Comment | Organism |
---|---|---|
physiological function | pyrrolysyl-tRNA synthetase is an atypical enzyme responsible for charging tRNAPyl with pyrrolysine, despite lacking precise tRNA anticodon recognition, the protein exhibits allosteric regulation of function, like any other tRNA synthetases | Desulfitobacterium hafniense |