6.1.1.11: serine-tRNA ligase
This is an abbreviated version!
For detailed information about serine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.11
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6.1.1.11
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raman
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surface-enhanced
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nanoparticles
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silver
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aminoacyl-trna
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aminoacylation
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serylation
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colloid
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selenocysteine
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anticodon
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trnasec
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asprs
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isoacceptors
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aarss
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lysyl-trna
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roughened
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phenylalanyl-trna
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trnatyr
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langmuir-blodgett
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alanyl-trna
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handheld
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albomycins
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citrate-reduced
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molecular biology
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nanostars
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selenophosphate
- 6.1.1.11
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raman
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surface-enhanced
- nanoparticles
- silver
- aminoacyl-trna
- aminoacylation
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serylation
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colloid
- selenocysteine
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anticodon
- trnasec
- asprs
-
isoacceptors
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aarss
- lysyl-trna
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roughened
- phenylalanyl-trna
- trnatyr
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langmuir-blodgett
- alanyl-trna
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handheld
- albomycins
-
citrate-reduced
- molecular biology
-
nanostars
- selenophosphate
Reaction
Synonyms
62 kDa RNA-binding protein, bacterial SerRS, bacterial type seryl-tRNA synthetase, bacterial-type SerRS, bMbSerRS, methanogenic SerRS, methanogenic type seryl-tRNA synthetase, methanogenic-type SerRS, methanogenic-type SerRSs, methanogenic-type seryl-tRNA synthetase, mMbSerRS, mSerRS, mtSerRS, SARS, SCSerS, Serine transfer RNA synthetase, Serine translase, Serine--tRNA ligase, SerRS, SerRS1, SerRS2, SerRSmt, serS, SERSEC, seryl tRNA synthetase, Seryl-transfer ribonucleate synthetase, Seryl-transfer ribonucleic acid synthetase, Seryl-transfer RNA synthetase, Seryl-tRNA synthetase, seryl-tRNA synthetase 1, seryl-tRNA synthetase 2, seryl-tRNA-synthetase, SerZMo, STS, subclass IIa dimeric SerRS, SvsR, Synthetase, seryl-transfer ribonucleate, tRNASer/seryl-tRNA synthetase, ttSerRS, TT_C0520, VlmL, ZmSerS
ECTree
6.1.1.11 serine-tRNA ligaseAdvanced search results
results (
results (KM Value
KM Value on EC 6.1.1.11 - serine-tRNA ligase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2.35
DL-Serine hydroxamate
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in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
29
L-cysteine
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in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
2 - 3.4
L-threonine
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in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.0013
ATP
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ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in presence of tRNASer
0.051
L-Ser
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mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.108
L-Ser
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mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
0.145
L-Ser
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mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
0.016
L-serine
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wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.0257
L-serine
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mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.049
L-serine
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mutant enzyme Q400A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.0731
L-serine
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mutant enzyme H250A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.18
L-serine
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in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.2491
L-serine
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mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.45
L-serine
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mitochondrial isozyme, ATP-diphosphate exchange reaction, pH 7.5, 30°C
0.5
L-serine
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ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in absence of tRNASer
0.9
L-serine
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mutant enzyme F397P/A399G, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C
0.45 - 0.89
Ser
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serine-dependent ATP-diphosphate exchange, mutant enzymes
0.00004
tRNASer
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wild-type enzyme, mutant SerRS11, and mutant SerRS12, pH 7.2, 30°C
0.00013
tRNASer
mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C
0.00065
tRNASer
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mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA
0.00065
tRNASer
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mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA
0.00066
tRNASer
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mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA
0.0008628
tRNASer
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in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.002
tRNASer
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pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS
additional information
additional information
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a temperature-dependent inhibition by conformational change of the enzyme (50°C-70°C) lowers both the catalytic activity and the substrate affinity of the ATP and amino acid sites as indicated by a sharp rise in Km with temperature
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additional information
additional information
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Lineweaver-Burk plots for Ser and tRNASer are non-linear
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additional information
additional information
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Km values for tRNASer transcripts
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additional information
additional information
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kinetic changes in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay
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additional information
additional information
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kinetics for the ATP-diphosphate exchange reaction
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additional information
additional information
kinetics with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
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additional information
additional information
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kinetics with diverse mutant variants of tRNASerUGA and tRNASerGCU with the recombinant mitochondrial isozyme, overview
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additional information
additional information
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Km-values for different tRNASer variants
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additional information
additional information
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calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
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additional information
additional information
calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
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additional information
additional information
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calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview
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additional information
additional information
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addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview
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