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Literature summary extracted from

  • Druart, K.; Guennec, M.L.; Palmai, Z.; Simonson, T.
    Probing the stereospecificity of tyrosyl- and glutaminyl-tRNA synthetase with molecular dynamics (2017), J. Mol. Graph. Model., 71, 192-199 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.1 D81R site-diretced mutagenesis, the mutant shows reduced stereospecificity for L-Tyr compared to wild-type Methanocaldococcus jannaschii
6.1.1.1 E36Q site-diretced mutagenesis, the mutant shows increased, but not inverted, stereospecificity for L-Tyr compared to wild-type Methanocaldococcus jannaschii
6.1.1.18 D81Q site-diretced mutagenesis, the mutant has and increased, inverted stereospecificity. D81Q is predicted to lead to a rotated ligand backbone and an increased, not a decreased L-Tyr preference Escherichia coli
6.1.1.18 R260Q site-diretced mutagenesis, mutating Arg260 to the homologous but neutral Gln does not reduce the L-GlnAMP preference, instead, the mutation produces a change in the DELTADELTAG value that is much smaller than the wild-type free energy component Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.1 Mg2+ required Methanocaldococcus jannaschii
6.1.1.18 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.1 ATP + L-tyrosine + tRNATyr Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln Escherichia coli
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.1 Methanocaldococcus jannaschii Q57834 i.e. Methanocaldococcus jannaschii
-
6.1.1.1 Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440 Q57834 i.e. Methanocaldococcus jannaschii
-
6.1.1.18 Escherichia coli P00962
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.1 ATP + L-tyrosine + tRNATyr
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr
-
 Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 additional information enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA Methanocaldococcus jannaschii ?
-
 ?
6.1.1.1 additional information enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440 ?
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 additional information GlnRS has adetectable tRNA-acylation activity for its D-amino acid substrate Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.1 class I tyrosyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
6.1.1.1 Tyrosyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
6.1.1.1 TyrRS
-
 Methanocaldococcus jannaschii
6.1.1.18 class I glutaminyl-tRNA synthetase
-
 Escherichia coli
6.1.1.18 GlnRS
-
 Escherichia coli
6.1.1.18 Glutaminyl-tRNA synthetase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.1 ATP
-
 Methanocaldococcus jannaschii
6.1.1.18 ATP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
6.1.1.1 evolution the enzyme belongs to the class I aminoacyl-tRNA synthetase family Methanocaldococcus jannaschii
6.1.1.1 additional information molecular dynamics modeling of substrates L- and D-Tyr into the active site of wild-type enzyme and mutants D81R and E36Q using the PDB ID 1J1U X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview Methanocaldococcus jannaschii
6.1.1.18 evolution the enzyme belongs to the class I aminoacyl-tRNA synthetase family Escherichia coli
6.1.1.18 additional information molecular dynamics modeling of L-GlnAMP using the PDB ID 1QTQ X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview Escherichia coli