EC Number   |
Natural Substrates |
|---|
   6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
- |
| 6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo |
| 6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
Pyl-tRNAPyl insertion at UAG, a specialized mRNA motif is not essential for stopcodon recoding, unlike for selenocysteine incorporation |
| 6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
pyrrolysyl-tRNA synthetase PylRS attaches L-pyrrolysine to its cognate tRNA, the special amber suppressor tRNAPyl, encoded by gene pylT |
| 6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
the enzyme attaches attaches L-pyrrolysine only to tRNA transcripts with a 3'-OH group at A76, whereas no aminoacylation at the 2'-OH group is detected |
| 6.1.1.26 | ATP + L-pyrrolysine + tRNAPyl |
the enzyme attaches L-pyrrolysine only to tRNA transcripts with a 3'-OH group at A76, whereas no aminoacylation at the 2'-OH group is detected |
| 6.1.1.26 | more |
enzyme evolution study, PylRS can be placed in the aminoacyl-tRNA synthetase tree as the last known synthetase that evolved for genetic code expansion, pyrrolysine arose before the last universal common ancestral state |
| 6.1.1.26 | more |
Methanosarcina cells have two pathways for acylating the suppressor tRNAPyl to ensure efficient translation of the in-frame UAG codon in case of pyrrolysine deficiency and safeguard the biosynthesis of the proteins whose genes contain this special codon, L-pyrrolysine is found in the Methanosarcina barkeri monomethylamine methyltransferase protein in a position that is encoded by an in-frame UAG stop codon in the mRNA, overview |
| 6.1.1.26 | more |
pyrrolysine is required in e.g. methylamine methyltransferase MtmB, overview |
| 6.1.1.26 | more |
the amino-terminal extension present in archaeal PylRSs is dispensable for in vitro activity, but required for PylRS function in vivo |
