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Literature summary extracted from

  • Oki, K.; Sakamoto, K.; Kobayashi, T.; Sasaki, H.M.; Yokoyama, S.
    Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog (2008), Proc. Natl. Acad. Sci. USA, 105, 13298-13303.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.20 expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Eed-IYRS, overview Escherichia coli
6.1.1.20 expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ped-IYRS, overview Pyrococcus horikoshii
6.1.1.20 expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ted-IYRS, overview Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.20 additional information the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview Thermus thermophilus
6.1.1.20 additional information the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview Escherichia coli
6.1.1.20 additional information the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.20 Mg2+
-
 Thermus thermophilus
6.1.1.20 Mg2+
-
 Escherichia coli
6.1.1.20 Mg2+
-
 Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.20 ATP + L-phenylalanine + tRNAPhe Thermus thermophilus
-
 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
6.1.1.20 ATP + L-phenylalanine + tRNAPhe Escherichia coli
-
 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
6.1.1.20 ATP + L-phenylalanine + tRNAPhe Pyrococcus horikoshii
-
 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.20 Escherichia coli
-
-
-
6.1.1.20 Pyrococcus horikoshii
-
-
-
6.1.1.20 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
 Thermus thermophilus AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
 Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
 Pyrococcus horikoshii AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
6.1.1.20 additional information editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview Thermus thermophilus ?
-
 ?
6.1.1.20 additional information editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview Escherichia coli ?
-
 ?
6.1.1.20 additional information editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview Pyrococcus horikoshii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.20 tetramer PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
6.1.1.20 Phenylalanyl-tRNA synthetase
-
 Thermus thermophilus
6.1.1.20 Phenylalanyl-tRNA synthetase
-
 Escherichia coli
6.1.1.20 Phenylalanyl-tRNA synthetase
-
 Pyrococcus horikoshii
6.1.1.20 PheRS
-
 Thermus thermophilus
6.1.1.20 PheRS
-
 Escherichia coli
6.1.1.20 PheRS
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.20 37
-
 assay at Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.20 7.5
-
 assay at Pyrococcus horikoshii

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.20 ATP
-
 Thermus thermophilus
6.1.1.20 ATP
-
 Escherichia coli
6.1.1.20 ATP
-
 Pyrococcus horikoshii