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Literature summary for 6.1.1.3 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)

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

Protein Variants

Protein Variants Comment Organism
D180A charging of tRNAThr with serine, mutant is no longer able to rapidly deacetylate Ser-tRNAThr Escherichia coli
H73A/H77A charging of tRNAThr with serine, mutant is no longer able to deacetylate Ser-tRNAThr Escherichia coli
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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
class II enzyme
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNAThr very low activity with the wild-type enzyme Escherichia coli AMP + diphosphate + L-seryl-tRNAThr
-
?
ATP + L-threonine + tRNAThr
-
Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli