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Literature summary for 6.1.1.26 extracted from

  • Bhattacharyya, M.; Vishveshwara, S.
    Probing the allosteric mechanism in pyrrolysyl-tRNA synthetase using energy-weighted network formalism (2011), Biochemistry, 50, 6225-6236.
    View publication on PubMed
Search for more literature for 6.1.1.26

Organism

Organism UniProt Comment Textmining
Desulfitobacterium hafniense
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information molecular dynamics simulations of the structures of PylRS and its complexes with tRNAPyl and activated pyrrolysine, overview. Identification of key residues and interactions leading to shortest paths of communication in the structure networks of DhPylRS. Dimeric hPylRS in different states of ligation: Sys1 as native DhPylRS, Sys2 as DhPylRS-Pyl-AMP, and Sys3 as DhPylRS-Pyl-AMP-tRNA, detailed overview Desulfitobacterium hafniense ?
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Subunits

Subunits Comment Organism
dimer molecular dynamics simulations of the structures of PylRS and its complexes with tRNAPyl and activated pyrrolysine, overview. Identification of key residues and interactions leading to shortest paths of communication in the structure networks of DhPylRS. Dmeric hPylRS in different states of ligation: Sys1 as native DhPylRS, Sys2 as DhPylRS-Pyl-AMP, and Sys3 as DhPylRS-Pyl-AMP-tRNA, detailed overview Desulfitobacterium hafniense

Synonyms

Synonyms Comment Organism
PylRS
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 Desulfitobacterium hafniense
pyrrolysyl-tRNA synthetase
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 Desulfitobacterium hafniense

General Information

General Information Comment Organism
physiological function 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 Desulfitobacterium hafniense