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Literature summary for 6.1.1.1 extracted from

  • Sun, R.; Zheng, H.; Fang, Z.; Yao, W.
    Rational design of aminoacyl-tRNA synthetase specific for p-acetyl-L-phenylalanine (2010), Biochem. Biophys. Res. Commun., 391, 709-715.
    View publication on PubMed
Search for more literature for 6.1.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
additional information 60 aminoacyl-tRNA synthetases are modeled using the conformation of Methanococcus jannaschii tRNATyr/tyrosyl-tRNA synthetase as template Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-tyrosine + tRNATyr Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q57834
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tyrosine + tRNATyr
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
ATP + p-acetyl-L-phenylalanine + tRNATyr aminoacyl-tRNA synthetases are designed through a combination of homology modeling, molecular docking and binding affinity computation with the purpose of incorporating pACPhe into proteins in Escherichia coli Methanocaldococcus jannaschii AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
-
 ?

Synonyms

Synonyms Comment Organism
tRNATyr/tyrosyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
Tyrosyl-tRNA synthetase
-
 Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Methanocaldococcus jannaschii