6.1.1.26: pyrrolysine-tRNAPyl ligase
This is an abbreviated version!
For detailed information about pyrrolysine-tRNAPyl ligase, go to the full flat file.
Word Map on EC 6.1.1.26
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6.1.1.26
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synthetases
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methanosarcina
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amber
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aminoacylation
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mazei
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ncaas
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anticodon
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aarss
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barkeri
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pylts
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histidyl-trnas
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hisrs
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hafniense
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desulfitobacterium
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methanosarcinaceae
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trnacua
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phers
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phenylalanyl-trna
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seryl-trna
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non-cognate
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glyrs
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molecular biology
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synthesis
- 6.1.1.26
- synthetases
- methanosarcina
-
amber
- aminoacylation
- mazei
-
ncaas
-
anticodon
-
aarss
- barkeri
-
pylts
-
histidyl-trnas
- hisrs
- hafniense
- desulfitobacterium
- methanosarcinaceae
-
trnacua
- phers
- phenylalanyl-trna
- seryl-trna
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non-cognate
- glyrs
- molecular biology
- synthesis
Reaction
Synonyms
class II aminoacyl-tRNA synthetase, DhaPylSc, LysZ-RS, More, PylRS, PylS, PylSc, PylSn, pyrrolysyl-tRNA synthetase
ECTree
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Application
Application on EC 6.1.1.26 - pyrrolysine-tRNAPyl ligase
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molecular biology
synthesis
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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
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the pyrrolysyl-tRNA synthetase/tRNAPyl suppression system can be used for the in vitro synthesis of peptides with nonnatural backbones
molecular 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