Literature summary for 6.1.1.3 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.

Search for more literature for 6.1.1.3

Cloned(Commentary)

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

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

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 [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

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/ Products (Substrates)

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

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

Purification (Commentary)

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 and Products (Substrate)

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

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 [°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 [1/s]

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

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

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 [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

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Release 2023.1 (January 2023)