Cloned (Comment) | Organism |
---|---|
expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis | Saccharolobus solfataricus |
expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis | Methanocaldococcus jannaschii |
expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis | Archaeoglobus fulgidus |
expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis | Halobacterium sp. |
expression of His-tagged wild-type and mutant enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D435A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
H309A | site-directed mutagenesis, mutant shows highly increased Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
H337A | site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
L489W | site-directed mutagenesis, mutant has a reduced space of the hydrophobic cluster near the active site resulting in a 1500fold increase in Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
P296A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
P296S | site-directed mutagenesis, mutant shows slightly increased Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
P335A | site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
P464A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
R282A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
S429A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
T307A | site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
Y313A | site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
borrelidin | inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Archaeoglobus fulgidus | |
borrelidin | slowly but tight binding, noncompetitive with respect to threonine and ATP, inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Escherichia coli | |
borrelidin | inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Halobacterium sp. | |
borrelidin | inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Helicobacter pylori | |
borrelidin | inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Methanocaldococcus jannaschii | |
borrelidin | inhibition mechanism via conformational change abolishing the activation of threonine, a unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases of different origin, comparison, overview | Saccharolobus solfataricus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | presteady-state and steady-state kinetic measurement | Escherichia coli | |
additional information | - |
additional information | steady-state kinetic measurement | Saccharolobus solfataricus | |
additional information | - |
additional information | steady-state kinetic measurement | Methanocaldococcus jannaschii | |
additional information | - |
additional information | steady-state kinetic measurement | Archaeoglobus fulgidus | |
additional information | - |
additional information | steady-state kinetic measurement | Halobacterium sp. | |
0.09 | - |
L-threonine | pH 7.5, 65°C, wild-type enzyme | Archaeoglobus fulgidus | |
0.1 | - |
L-threonine | pH 7.5, 55°C, wild-type enzyme | Saccharolobus solfataricus | |
0.1 | - |
L-threonine | pH 7.5, 65°C, wild-type enzyme | Methanocaldococcus jannaschii | |
0.11 | - |
L-threonine | pH 7.5, 37°C, wild-type enzyme | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Saccharolobus solfataricus | |
Mg2+ | - |
Methanocaldococcus jannaschii | |
Mg2+ | - |
Archaeoglobus fulgidus | |
Mg2+ | - |
Halobacterium sp. | |
Mg2+ | - |
Escherichia coli | |
Zn2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | Helicobacter pylori | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | Saccharolobus solfataricus | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | Methanocaldococcus jannaschii | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | Archaeoglobus fulgidus | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | Halobacterium sp. | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Escherichia coli | P0A8M3 | - |
- |
Halobacterium sp. | - |
- |
- |
Helicobacter pylori | - |
- |
- |
Methanocaldococcus jannaschii | - |
- |
- |
Saccharolobus solfataricus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography | Saccharolobus solfataricus |
recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography | Methanocaldococcus jannaschii |
recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography | Archaeoglobus fulgidus |
recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography | Halobacterium sp. |
recombinant His-tagged wild-type and mutant enzyme from Escherichia coli mutant by nickel affinity chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | - |
Helicobacter pylori | AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | - |
Saccharolobus solfataricus | AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | - |
Methanocaldococcus jannaschii | AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | - |
Archaeoglobus fulgidus | AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | - |
Halobacterium sp. | AMP + diphosphate + L-threonyl-tRNAThr | - |
r | |
ATP + L-threonine + tRNAThr | - |
Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
r |
Synonyms | Comment | Organism |
---|---|---|
Threonyl-tRNA synthetase | - |
Helicobacter pylori |
Threonyl-tRNA synthetase | - |
Saccharolobus solfataricus |
Threonyl-tRNA synthetase | - |
Methanocaldococcus jannaschii |
Threonyl-tRNA synthetase | - |
Archaeoglobus fulgidus |
Threonyl-tRNA synthetase | - |
Halobacterium sp. |
Threonyl-tRNA synthetase | - |
Escherichia coli |
ThrRS | - |
Helicobacter pylori |
ThrRS | - |
Saccharolobus solfataricus |
ThrRS | - |
Methanocaldococcus jannaschii |
ThrRS | - |
Archaeoglobus fulgidus |
ThrRS | - |
Halobacterium sp. |
ThrRS | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
presteady-state, assay at | Escherichia coli |
37 | - |
assay at | Halobacterium sp. |
37 | - |
steady-state, assay at | Escherichia coli |
55 | - |
assay at | Saccharolobus solfataricus |
65 | - |
assay at | Methanocaldococcus jannaschii |
65 | - |
assay at | Archaeoglobus fulgidus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.2 | - |
L-threonine | pH 7.5, 65°C, wild-type enzyme | Methanocaldococcus jannaschii | |
3.8 | - |
L-threonine | pH 7.5, 65°C, wild-type enzyme | Archaeoglobus fulgidus | |
16 | - |
L-threonine | pH 7.5, 55°C, wild-type enzyme | Saccharolobus solfataricus | |
33 | - |
L-threonine | pH 7.5, 37°C, wild-type enzyme | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
presteady-state, assay at | Escherichia coli |
7.5 | - |
assay at | Saccharolobus solfataricus |
7.5 | - |
assay at | Methanocaldococcus jannaschii |
7.5 | - |
assay at | Archaeoglobus fulgidus |
7.5 | - |
assay at | Halobacterium sp. |
7.5 | - |
steady-state, assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
AMP | - |
Helicobacter pylori | |
AMP | - |
Saccharolobus solfataricus | |
AMP | - |
Methanocaldococcus jannaschii | |
AMP | - |
Archaeoglobus fulgidus | |
AMP | - |
Halobacterium sp. | |
AMP | - |
Escherichia coli | |
ATP | - |
Helicobacter pylori | |
ATP | - |
Saccharolobus solfataricus | |
ATP | - |
Methanocaldococcus jannaschii | |
ATP | - |
Archaeoglobus fulgidus | |
ATP | - |
Halobacterium sp. | |
ATP | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia coli | |
0.000004 | - |
borrelidin | pH 7.5, 37°C, wild-type enzyme | Escherichia coli | |
0.0000045 | - |
borrelidin | pH 7.5, 55°C, wild-type enzyme | Saccharolobus solfataricus | |
0.006 | - |
borrelidin | above, pH 7.5, 65°C, wild-type enzyme | Methanocaldococcus jannaschii | |
0.006 | - |
borrelidin | above, pH 7.5, 65°C, wild-type enzyme | Archaeoglobus fulgidus | |
0.006 | - |
borrelidin | pH 7.5, 37°C, mutant L489W | Escherichia coli |