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Literature summary for 6.1.1.20 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
Search for more literature for 6.1.1.20

Cloned(Commentary)

Cloned (Comment) Organism
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
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
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

Protein Variants Comment Organism
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Pyrococcus horikoshii
-
-
-
Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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