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EC Number Application Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.26molecular biology PylRS as aminoacyl-tRNA synthetase allows the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or alpha-hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs 744388
Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.26molecular biology the pyrrolysyl-tRNA synthetase/tRNAPyl suppression system can be used for the in vitro synthesis of peptides with nonnatural backbones 728143
Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.26synthesis synthesis and genetic incorporation of aliphatic azides and alkynes into proteins using the natural pyrrolysyl tRNA synthetase/tRNACUA pair and the efficient bio-orthogonal labeling of these amino acids using [3+2] cycloaddition, i.e. click chemistry. Escherichia coli transformed with pBKPylS10 encoding pyrrolysyl tRNA synthetase and pMyo4TAGPylT-his610 encoding tRNACUA and a C-terminally hexahistidine tagged myoglobin gene with an amber codon at position 4 incorporates (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid. The yield of protein containing (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid is not improved by efforts to evolve the enzyme but is increased 5fold by increasing the concentration of (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid 7.5fold 704197
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