EC Number   |
General Information |
Reference |
|---|
   6.1.1.26 | evolution |
sequence alignment indicated that full-length PylRS contains a C-terminal class II AARS catalytic core and an N-terminal domain that apparently does not share sequence homology with any structurally known protein domains. The three dimensional organization of the PylRS catalytic core resembles that of other synthetases from the Class II AARS family |
-, 744388 |
| 6.1.1.26 | more |
along with its special CUA anticodon for the recognition of amber codon, the pylT transcript, tRNAPyl, has a distinct anticodon stem of six base pairs instead of five base pairs as observed in most tRNAs, a single base between D and anticodon stems, a single base between D and acceptor stems, and a three-base small variable arm |
-, 744388 |
| 6.1.1.26 | physiological function |
pyrrolysine insertion is akin to natural suppression and unlike the active stop codon reassignment that is required for selenocysteine insertion. In Thg1, pyrrolysine is a dispensable residue that appears to confer no selective advantage |
706527 |
| 6.1.1.26 | 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 |
714264 |
| 6.1.1.26 | physiological function |
the genetic incorporation of the 22nd proteinogenic amino acid, pyrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl |
-, 744388 |
| 6.1.1.26 | physiological function |
the genetic incorporation of the 22nd proteinogenic amino acid, pyrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl. When D-ornithine is provided in the growth medium, the clustered genes of pylT, pylS, pylC, and pylD were able to mediate amber suppression, pylC and pylD gene products are able to synthesize desmethyl-Pyl from D-ornithine and lysine and that PylRS tolerates alternative substrates |
744388 |
