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
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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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General Information
General Information on EC 6.1.1.26 - pyrrolysine-tRNAPyl ligase
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evolution
physiological function
additional information
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
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
evolution
Methanosarcina mazei ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
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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
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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
physiological function
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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
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
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
physiological function
Methanosarcina mazei ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
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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
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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
additional information
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
additional information
Methanosarcina mazei ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
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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
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