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Literature summary extracted from

  • Dock-Bregeon, A.; Sankaranarayanan, R.; Romby, P.; Caillet, J.; Springer, M.; Rees, B.; Francklyn, C.S.; Ehresmann, C.; Moras, D.
    Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem (2000), Cell, 103, 877-884.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.3 lamdaN-threonine-tRNA ligase complexed with Ser-AMS, X-ray diffraction structure determination at 1.65 A resolution and analysis Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 D180A charging of tRNAThr with serine, mutant is no longer able to rapidly deacetylate Ser-tRNAThr Escherichia coli
6.1.1.3 H73A/H77A charging of tRNAThr with serine, mutant is no longer able to deacetylate Ser-tRNAThr Escherichia coli
6.1.1.3 additional information truncated lamdaN-enzyme mutant, lacking the N-terminal domains N1 and N2, produces Ser-tRNAThr, reduced activity and altered substrate recognition compared to the wild-type which does nearly not incorporate serine Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Zn2+ used to discriminate against the isosteric valine at the activation step 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
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Escherichia coli
-
class II enzyme
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.3 ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr functional mechanism and substrate recognition, editing model, 2 separate active sites for substrate binding, binding of tRNA is more specific than the binding of the amino acid 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 very low activity with the wild-type enzyme Escherichia coli AMP + diphosphate + L-seryl-tRNAThr
-
?
6.1.1.3 ATP + L-threonine + tRNAThr
-
Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 Synthetase, threonyl-transfer ribonucleate
-
Escherichia coli
6.1.1.3 Threonine translase
-
Escherichia coli
6.1.1.3 Threonine--tRNA ligase
-
Escherichia coli
6.1.1.3 Threonine-transfer ribonucleate synthetase
-
Escherichia coli
6.1.1.3 Threonyl-ribonucleic synthetase
-
Escherichia coli
6.1.1.3 Threonyl-transfer ribonucleate synthetase
-
Escherichia coli
6.1.1.3 Threonyl-transfer ribonucleic acid synthetase
-
Escherichia coli
6.1.1.3 Threonyl-transfer RNA synthetase
-
Escherichia coli
6.1.1.3 Threonyl-tRNA synthetase
-
Escherichia coli
6.1.1.3 ThrRS
-
Escherichia coli
6.1.1.3 TRS
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP
-
Escherichia coli