6.1.1.3: threonine-tRNA ligase
This is an abbreviated version!
For detailed information about threonine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.3
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6.1.1.3
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synthetases
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aminoacyl-trna
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aminoacylation
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threonylation
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anticodon
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aarss
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borrelidin
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phenylalanyl-trna
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isoacceptors
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misactivates
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noncognate
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alanyl-trna
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mischarged
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anticodon-binding
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hisrs
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anticodon-like
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mistranslation
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post-transfer
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diagnostics
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drug development
- 6.1.1.3
- synthetases
- aminoacyl-trna
- aminoacylation
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threonylation
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anticodon
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aarss
- borrelidin
- phenylalanyl-trna
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isoacceptors
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misactivates
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noncognate
- alanyl-trna
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mischarged
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anticodon-binding
- hisrs
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anticodon-like
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mistranslation
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post-transfer
- diagnostics
- drug development
Reaction
Synonyms
ApThrRS-1, ApThrRS-2, BaThrRS, EcThrRS, ectRNAThr, McThrRS, mitochondrial threonyl-tRNA synthetase, MJ1197, MmThrRS, More, Mst1, ScmtThrRS, SfThrRS-1, SfThrRS-2, Synthetase, threonyl-transfer ribonucleate, TarS, Thr-tRNA synthetase, Threonine translase, Threonine--tRNA ligase, Threonine-transfer ribonucleate synthetase, threonyl tRNA synthetase, Threonyl-ribonucleic synthetase, Threonyl-transfer ribonucleate synthetase, Threonyl-transfer ribonucleic acid synthetase, Threonyl-transfer RNA synthetase, Threonyl-tRNA synthetase, ThrRS, ThrRS1, ThrS, TRS
ECTree
6.1.1.3 threonine-tRNA ligaseAdvanced search results
results (
results (KM Value
KM Value on EC 6.1.1.3 - threonine-tRNA ligase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
120
L-serine
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in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
0.1
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
0.11
L-threonine
pH 7.2, 60°C, recombinant wild-type enzyme
0.3
L-threonine
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in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C
0.00013
tRNA1Thr
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mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.0002
tRNA1Thr
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mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00024
tRNA1Thr
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mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00024
tRNA1Thr
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mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00028
tRNA1Thr
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mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00029
tRNA1Thr
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wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.0003
tRNA1Thr
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mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.0003
tRNA1Thr
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mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00031
tRNA1Thr
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mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00031
tRNA1Thr
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mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00046
tRNA1Thr
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mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00047
tRNA1Thr
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mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00048
tRNA1Thr
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mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00049
tRNA1Thr
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mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00059
tRNA1Thr
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mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00083
tRNA1Thr
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mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00095
tRNA1Thr
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mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00027
tRNA2Thr
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mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00037
tRNA2Thr
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mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00044
tRNA2Thr
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mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00044
tRNA2Thr
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wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00049
tRNA2Thr
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mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00051
tRNA2Thr
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mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00059
tRNA2Thr
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mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00064
tRNA2Thr
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mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00069
tRNA2Thr
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mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00078
tRNA2Thr
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mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00083
tRNA2Thr
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mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00094
tRNA2Thr
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mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00123
tRNA2Thr
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mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.00139
tRNA2Thr
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mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.0014
tRNA2Thr
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mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication
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0.000037 - 0.00007
tRNAThr
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of Thermus thermophilus, , depending on temperature
additional information
additional information
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Km values of variants of tRNAThr transcripts
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additional information
additional information
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kinetics and kinetic mechanism
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additional information
additional information
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mutant enzymes complementing the null mutant
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additional information
additional information
kinetics of recombinant wild-type and mutant enzymes with threonine and serine
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additional information
additional information
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kinetics of recombinant wild-type and mutant enzymes with threonine and serine
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additional information
additional information
kinetics of recombinant wild-type and mutant enzymes with threonine and serine
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additional information
additional information
presteady-state and steady-state kinetic measurement
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additional information
additional information
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presteady-state and steady-state kinetic measurement
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additional information
additional information
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steady-state kinetic measurement
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additional information
additional information
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steady-state kinetic measurement
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additional information
additional information
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steady-state kinetic measurement
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additional information
additional information
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steady-state kinetic measurement
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additional information
additional information
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kinetics of diphosphate exchange activities and threonylation of tRNAThr of ThrRS with or without H2O2 treatment, overview
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additional information
additional information
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kinetics of MST1 with different tRNAs, overview
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additional information
additional information
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pre-steady-state kinetics, kinetics of ATPase activity in presence of 3-hydroxynorvaline, overview
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additional information
additional information
aminoacylation kinetics of ScmtThrRS for various tRNAThr1 mutants derived from U33a or G36, overview. Rate constants of AMP formation by chimeric mutant enzyme CmThrRS
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additional information
additional information
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aminoacylation kinetics of ScmtThrRS for various tRNAThr1 mutants derived from U33a or G36, overview. Rate constants of AMP formation by chimeric mutant enzyme CmThrRS
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additional information
additional information
enzyme kinetics and stopped-flow fluorescence analysis, Michaelis-Menten steady-state kinetics of recombinant wild-type and mutant enzymes
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additional information
additional information
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enzyme kinetics and stopped-flow fluorescence analysis, Michaelis-Menten steady-state kinetics of recombinant wild-type and mutant enzymes
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additional information
additional information
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kinetics of the enzyme for cognate Thr and noncognate Ser are determined with an ATP-phosphate exchange reaction
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