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Literature summary for 6.1.1.3 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
Search for more literature for 6.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
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)

Crystallization (Comment) Organism
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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
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

Organism UniProt Comment Textmining
Escherichia coli P0A8M3
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNAThr low activity Escherichia coli AMP + diphosphate + L-seryl-tRNAThr
-
 r
ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 r
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

Synonyms Comment Organism
Threonyl-tRNA synthetase
-
 Escherichia coli
ThrRS
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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