Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Li, M.; Zhang, J.; Liu, C.; Fang, B.; Wang, X.; Xiang, W.
    Identification of borrelidin binding site on threonyl-tRNA synthetase (2014), Biochem. Biophys. Res. Commun., 451, 485-490 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 gene thrS, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 E458D site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, mutant shows decreased apparent rate constants Escherichia coli
6.1.1.3 G459D site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, mutant shows decreased apparent rate constants Escherichia coli
6.1.1.3 P424K site-directed mutagenesis, the sensitivity of the mutant enzyme to borrelidin is reduced markedly compared to wild-type, the mutant shows decreased apparent rate constants Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.3 borrelidin is an 18-membered macrolide polyketide produced by several actinomycete bacteria of the Streptomyces spp.. Identification of borrelidin binding site on threonyl-tRNA synthetase, molecular docking, overview. Borrelidin binds the pocket outside but adjacent to the active site of ThrRS, consisting of residues Y313, R363, R375, P424, E458, G459, and K465. Borrelidin may induce the cleft closure, which blocks the release of Thr-AMP and phosphate, to inhibit activity of ThrRS rather than inhibit the binding of ATP and threonine Escherichia coli
6.1.1.3 additional information development of novel borrelidin derivatives and rational design of structure-based ThrRS inhibitors, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 additional information
-
additional information enzyme kinetics and stopped-flow fluorescence analysis, Michaelis-Menten steady-state kinetics of recombinant wild-type and mutant enzymes Escherichia coli
6.1.1.3 0.101
-
L-threonine pH 7.4, 30°C, recombinant mutant G459D Escherichia coli
6.1.1.3 0.104
-
L-threonine pH 7.4, 30°C, recombinant mutant E458D Escherichia coli
6.1.1.3 0.105
-
L-threonine pH 7.4, 30°C, recombinant wild-type enzyme Escherichia coli
6.1.1.3 0.108
-
L-threonine pH 7.4, 30°C, recombinant mutant P424K Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+ required 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 P0A8M3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.3 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Threonyl-tRNA synthetase
-
Escherichia coli
6.1.1.3 ThrRS
-
Escherichia coli
6.1.1.3 ThrS
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 30
-
assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 2 8 L-threonine pH 7.4, 30°C, recombinant mutant G459D Escherichia coli
6.1.1.3 30
-
L-threonine pH 7.4, 30°C, recombinant mutant P424K Escherichia coli
6.1.1.3 34
-
L-threonine pH 7.4, 30°C, recombinant mutant E458D Escherichia coli
6.1.1.3 35
-
L-threonine pH 7.4, 30°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 7.4
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP binding structure Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.3 0.0000034
-
borrelidin pH 7.4, 30°C, recombinant wild-type enzyme Escherichia coli
6.1.1.3 0.0000191
-
borrelidin pH 7.4, 30°C, recombinant mutant E458D Escherichia coli
6.1.1.3 0.0000651
-
borrelidin pH 7.4, 30°C, recombinant mutant P424K Escherichia coli
6.1.1.3 0.0001114
-
borrelidin pH 7.4, 30°C, recombinant mutant G459D Escherichia coli