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Literature summary extracted from

  • Ruan, B.; Bovee, M.L.; Sacher, M.; Stathopoulos, C.; Poralla, K.; Francklyn, C.S.; Soll, D.
    A unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases (2005), J. Biol. Chem., 280, 571-577.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis Saccharolobus solfataricus
6.1.1.3 expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis Methanocaldococcus jannaschii
6.1.1.3 expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis Archaeoglobus fulgidus
6.1.1.3 expression of His-tagged enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis Halobacterium sp.
6.1.1.3 expression of His-tagged wild-type and mutant enzyme in an enzyme-deficient Escherichia coli mutant, complementation analysis Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 D435A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 H309A site-directed mutagenesis, mutant shows highly increased Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 H337A site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 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
6.1.1.3 P296A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 P296S site-directed mutagenesis, mutant shows slightly increased Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 P335A site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 P464A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 R282A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 S429A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 T307A site-directed mutagenesis, mutant shows increased Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli
6.1.1.3 Y313A site-directed mutagenesis, mutant shows a similar Ki for inhibitor borrelidin compared to the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.3 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
6.1.1.3 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
6.1.1.3 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.
6.1.1.3 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
6.1.1.3 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
6.1.1.3 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 additional information
-
 additional information presteady-state and steady-state kinetic measurement Escherichia coli
6.1.1.3 additional information
-
 additional information steady-state kinetic measurement Saccharolobus solfataricus
6.1.1.3 additional information
-
 additional information steady-state kinetic measurement Methanocaldococcus jannaschii
6.1.1.3 additional information
-
 additional information steady-state kinetic measurement Archaeoglobus fulgidus
6.1.1.3 additional information
-
 additional information steady-state kinetic measurement Halobacterium sp.
6.1.1.3 0.09
-
 L-threonine pH 7.5, 65°C, wild-type enzyme Archaeoglobus fulgidus
6.1.1.3 0.1
-
 L-threonine pH 7.5, 55°C, wild-type enzyme Saccharolobus solfataricus
6.1.1.3 0.1
-
 L-threonine pH 7.5, 65°C, wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 0.11
-
 L-threonine pH 7.5, 37°C, wild-type enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+
-
 Saccharolobus solfataricus
6.1.1.3 Mg2+
-
 Methanocaldococcus jannaschii
6.1.1.3 Mg2+
-
 Archaeoglobus fulgidus
6.1.1.3 Mg2+
-
 Halobacterium sp.
6.1.1.3 Mg2+
-
 Escherichia coli
6.1.1.3 Zn2+
-
 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 Helicobacter pylori
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Saccharolobus solfataricus
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Archaeoglobus fulgidus
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Halobacterium sp.
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Archaeoglobus fulgidus
-
-
-
6.1.1.3 Escherichia coli P0A8M3
-
-
6.1.1.3 Halobacterium sp.
-
-
-
6.1.1.3 Helicobacter pylori
-
-
-
6.1.1.3 Methanocaldococcus jannaschii
-
-
-
6.1.1.3 Saccharolobus solfataricus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.3 recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography Saccharolobus solfataricus
6.1.1.3 recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography Methanocaldococcus jannaschii
6.1.1.3 recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography Archaeoglobus fulgidus
6.1.1.3 recombinant His-tagged enzyme from Escherichia coli mutant by nickel affinity chromatography Halobacterium sp.
6.1.1.3 recombinant His-tagged wild-type and mutant enzyme from Escherichia coli mutant 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
-
 Helicobacter pylori AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Saccharolobus solfataricus AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Archaeoglobus fulgidus AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Halobacterium sp. AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 r

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 Threonyl-tRNA synthetase
-
 Helicobacter pylori
6.1.1.3 Threonyl-tRNA synthetase
-
 Saccharolobus solfataricus
6.1.1.3 Threonyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
6.1.1.3 Threonyl-tRNA synthetase
-
 Archaeoglobus fulgidus
6.1.1.3 Threonyl-tRNA synthetase
-
 Halobacterium sp.
6.1.1.3 Threonyl-tRNA synthetase
-
 Escherichia coli
6.1.1.3 ThrRS
-
 Helicobacter pylori
6.1.1.3 ThrRS
-
 Saccharolobus solfataricus
6.1.1.3 ThrRS
-
 Methanocaldococcus jannaschii
6.1.1.3 ThrRS
-
 Archaeoglobus fulgidus
6.1.1.3 ThrRS
-
 Halobacterium sp.
6.1.1.3 ThrRS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 30
-
 presteady-state, assay at Escherichia coli
6.1.1.3 37
-
 assay at Halobacterium sp.
6.1.1.3 37
-
 steady-state, assay at Escherichia coli
6.1.1.3 55
-
 assay at Saccharolobus solfataricus
6.1.1.3 65
-
 assay at Methanocaldococcus jannaschii
6.1.1.3 65
-
 assay at Archaeoglobus fulgidus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 1.2
-
 L-threonine pH 7.5, 65°C, wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 3.8
-
 L-threonine pH 7.5, 65°C, wild-type enzyme Archaeoglobus fulgidus
6.1.1.3 16
-
 L-threonine pH 7.5, 55°C, wild-type enzyme Saccharolobus solfataricus
6.1.1.3 33
-
 L-threonine pH 7.5, 37°C, wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 7.4
-
 presteady-state, assay at Escherichia coli
6.1.1.3 7.5
-
 assay at Saccharolobus solfataricus
6.1.1.3 7.5
-
 assay at Methanocaldococcus jannaschii
6.1.1.3 7.5
-
 assay at Archaeoglobus fulgidus
6.1.1.3 7.5
-
 assay at Halobacterium sp.
6.1.1.3 7.5
-
 steady-state, assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 AMP
-
 Helicobacter pylori
6.1.1.3 AMP
-
 Saccharolobus solfataricus
6.1.1.3 AMP
-
 Methanocaldococcus jannaschii
6.1.1.3 AMP
-
 Archaeoglobus fulgidus
6.1.1.3 AMP
-
 Halobacterium sp.
6.1.1.3 AMP
-
 Escherichia coli
6.1.1.3 ATP
-
 Helicobacter pylori
6.1.1.3 ATP
-
 Saccharolobus solfataricus
6.1.1.3 ATP
-
 Methanocaldococcus jannaschii
6.1.1.3 ATP
-
 Archaeoglobus fulgidus
6.1.1.3 ATP
-
 Halobacterium sp.
6.1.1.3 ATP
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.3 additional information
-
 additional information
-
 Escherichia coli
6.1.1.3 0.000004
-
 borrelidin pH 7.5, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 0.0000045
-
 borrelidin pH 7.5, 55°C, wild-type enzyme Saccharolobus solfataricus
6.1.1.3 0.006
-
 borrelidin above, pH 7.5, 65°C, wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 0.006
-
 borrelidin above, pH 7.5, 65°C, wild-type enzyme Archaeoglobus fulgidus
6.1.1.3 0.006
-
 borrelidin pH 7.5, 37°C, mutant L489W Escherichia coli