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Literature summary extracted from

  • Dock-Bregeon, A.C.; Rees, B.; Torres-Larios, A.; Bey, G.; Caillet, J.; Moras, D.
    Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution (2004), Mol. Cell, 16, 375-386.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 expression of non-tagged N1 and N2 domains comprising residues 1-65 and 66-225 in one fragment in strain BL21 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.3 purified recombinant N-terminal part of the enzyme, i.e. N1 and N2 domains comprising residues 1-65 and 66-225 in one fragment, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modeling Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.3 Zn2+ inhibits the editing reaction Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+
-
 Escherichia coli
6.1.1.3 Zn2+ assures that no valine is bound Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 additional information Escherichia coli the enzyme needs to discriminate between threonine, serine, and valine in vivo, mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Escherichia coli P0A8M3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.3 recombinant non-tagged N1 and N2 domains comprising residues 1-65 and 66-225 in one fragment by ion exchange chromatography, ammonium sulfate fractionation, hydrophobic interaction chromatography, and ultrafiltration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + L-serine + tRNAThr low activity Escherichia coli AMP + diphosphate + L-seryl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 additional information the enzyme needs to discriminate between threonine, serine, and valine in vivo, mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution, overview Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 Threonyl-tRNA synthetase
-
 Escherichia coli
6.1.1.3 ThrRS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 37
-
 aminoacylation assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 7.7
-
 aminoacylation assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 AMP
-
 Escherichia coli
6.1.1.3 ATP
-
 Escherichia coli
6.1.1.3 additional information cofactor binding structure, modeling Escherichia coli