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ProteomicsChimeric design of Pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion
An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a key prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic code ex...
ORGANISM(S): Escherichia coli 
2020-05-25 | PXD018660 | Pride
Chimeric design Genetic code expansion 
ProteomicsCharacterization of two mutually orthogonal pyrrolysyl-tRNA synthetase/tRNAPyl pairs residing in the same organism
Site-specific incorporation of distinct non-canonical amino acids (ncAAs) into proteins via genetic code expansion requires mutually orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs. Pyrrolysyl–tRNA synthetase (PylRS)/tRNAPyl pairs are ideal for genetic code expansion and have been extensively...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2022-05-12 | PXD027053 | Pride
Mutually orthogonal Pyrrolysyl-trna synthetase Archaea Trnapyl Genetic code expansion 
UnknownMutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs.
Not available
S-EPMC6055992 | biostudies-literature
UnknownQuintuply orthogonal pyrrolysyl-tRNA synthetase/tRNAPyl pairs.
Not available
S-EPMC7615293 | biostudies-literature
UnknownPyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function.
Not available
S-EPMC3778162 | biostudies-literature
UnknownA rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum.
Not available
S-EPMC3288562 | biostudies-literature
UnknownPyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.
Not available
S-EPMC5321558 | biostudies-literature
ProteomicsMachine learning-guided evolution of pyrrolysyl-tRNA synthetase for improved incorporation efficiency of diverse noncanonical amino acids
The pyrrolysyl-tRNA synthetase (PylRS) is widely used to incorporate noncanonical amino acids (ncAAs) into proteins. However, most of ncAA-containing protein yields remain low due to the limited activity of PylRS variants. Here, we apply machine learning (ML) to engineer the tRNA-binding domain of P...
ORGANISM(S): Escherichia coli 
2025-07-25 | PXD065336 | Pride
Lc-ms Sfgfp Noncanonical amino acids 
UnknownExpanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair.
Not available
S-EPMC2956376 | biostudies-literature
UnknownPyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality.
Not available
S-EPMC2648862 | biostudies-literature
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