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Literature summary for 6.1.1.26 extracted from

  • Kobayashi, T.; Yanagisawa, T.; Sakamoto, K.; Yokoyama, S.
    Recognition of non-alpha-amino substrates by pyrrolysyl-tRNA synthetase (2009), J. Mol. Biol., 385, 1352-1360.
    View publication on PubMed
Search for more literature for 6.1.1.26

Application

Application Comment Organism
molecular biology the pyrrolysyl-tRNA synthetase/tRNAPyl suppression system can be used for the in vitro synthesis of peptides with nonnatural backbones Methanosarcina mazei

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanosarcina mazei

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structures of the enzyme reveals that it has a unique, large pocket for amino acid binding Methanosarcina mazei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-pyrrolysine + tRNAPyl Methanosarcina mazei
-
 AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina mazei
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-pyrrolysine + tRNAPyl
-
 Methanosarcina mazei AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
 ?
ATP + L-pyrrolysine + tRNAPyl the wild type enzyme recognizes the natural lysine derivative as well as many lysine analogs, including Nepsilon-(tert-butoxycarbonyl)-L-lysine (Boc-lysine), with diverse side chain sizes and structures Methanosarcina mazei AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
 ?

Synonyms

Synonyms Comment Organism
PylRS
-
 Methanosarcina mazei
pyrrolysyl-tRNA synthetase
-
 Methanosarcina mazei