6.1.1.1: tyrosine-tRNA ligase
This is an abbreviated version!
For detailed information about tyrosine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.1
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6.1.1.1
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synthetases
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aminoacylation
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tyrosylation
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stearothermophilus
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anticodon
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amber
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jannaschii
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trprs
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aarss
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methanococcus
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kmsks
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tryptophanyl-trna
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charcot-marie-tooth
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mischarging
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trna-like
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d-tyrosine
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self-splicing
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methanocaldococcus
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half-of-the-sites
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elr
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non-cognate
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methionyl-trna
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isoleucyl-trna
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medicine
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biotechnology
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sideroblastic
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anticodon-binding
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tyrts
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3-iodo-l-tyrosine
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glycyl-trna
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drug development
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pharmacology
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leurs
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misacylation
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phenylalanyl-trna
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fersht
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brome
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hisrs
- 6.1.1.1
- synthetases
- aminoacylation
-
tyrosylation
- stearothermophilus
-
anticodon
-
amber
- jannaschii
- trprs
-
aarss
- methanococcus
-
kmsks
-
tryptophanyl-trna
-
charcot-marie-tooth
-
mischarging
-
trna-like
- d-tyrosine
-
self-splicing
- methanocaldococcus
-
half-of-the-sites
- elr
-
non-cognate
- methionyl-trna
-
isoleucyl-trna
- medicine
- biotechnology
-
sideroblastic
-
anticodon-binding
-
tyrts
- 3-iodo-l-tyrosine
- glycyl-trna
- drug development
- pharmacology
- leurs
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misacylation
- phenylalanyl-trna
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fersht
-
brome
- hisrs
Reaction
Synonyms
CHOTyrRS, class I tyrosyl-tRNA synthetase, CYT-18, CYT-18 protein, dTyRS, hTyrRS, LdTyrRS, LMJF_14_1370, mini-tyrosyl-tRNA synthetase, mini-TyrRS, mitochondrial tyrosyl-tRNA synthetase, MjYRS, mt-TyrRS, mtTyrRS, NpAla TyrRS, p-BrPhe TyrRS, tRNATyr/tyrosyl-tRNA synthetase, Tyrosine translase, Tyrosine tRNA synthetase, Tyrosine--tRNA ligase, Tyrosine-transfer ribonucleate synthetase, Tyrosine-transfer RNA ligase, tyrosyl aminoacyl-tRNA synthetase, tyrosyl synthetase, tyrosyl tRNA synthetase, Tyrosyl--tRNA ligase, Tyrosyl-transfer ribonucleate synthetase, Tyrosyl-transfer ribonucleic acid synthetase, Tyrosyl-transfer RNA synthetase, Tyrosyl-tRNA ligase, Tyrosyl-tRNA synthetase, tyrosyl—tRNA synthetase, TyrRS, TyrRSs, TyrRZ, tyrS, TYS1, YARS, YRS, YTS
ECTree
6.1.1.1 tyrosine-tRNA ligaseAdvanced search results
results (
results (KM Value
KM Value on EC 6.1.1.1 - tyrosine-tRNA ligase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.00043
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00045
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00049
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00071
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.00223
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.07
ATP
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phosphate exchange reaction, pH 8.0, wild-type enzyme
0.018
L-beta-(5-hydroxy-2-pyridyl)-alanine
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wild-type enzyme, pH 7.5, 30°C
0.0021
L-tyrosine
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wild-type enzyme and mutant L105V, pH 7.8, 25°C
0.00669
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00678
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00713
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00728
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00845
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.012
L-tyrosine
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pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
0.014
L-tyrosine
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pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
0.021
L-tyrosine
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phosphate exchange reaction, pH 8.0, wild-type enzyme
0.027
L-tyrosine
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aminoacylation reaction, pH 8.0, wild-type enzyme
0.00022
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
0.00037
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.00042
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00045
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00048
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.0025
tRNATyr
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aminoacylation reaction, pH 8.0, wild-type enzyme
0.00068
tRNATyr(G34C)
37°C, pH 7.5, mutant enzyme D268R
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0.00035
tRNATyr(wild-type)
37°C, pH 7.5, wild-type enzyme
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0.0014
tRNATyr(wild-type)
37°C, pH 7.5, mutant enzyme D268R
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additional information
additional information
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role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
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additional information
additional information
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role of threonine 234 in catalysis
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additional information
additional information
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kinetic analysis of mutation
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additional information
additional information
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role of lysine 233 in catalysis
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additional information
additional information
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stoichiometry of substrate binding
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additional information
additional information
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energy profiles for wild-type and mutant enzymes, kinetics for the second reaction step: wild-type enzyme and mutants D78A, Y169A, Q173A, D194A, and Q195A, kinetics for the first reaction step: wild-type enzyme, and mutants D194A and Q195A
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additional information
additional information
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fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
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additional information
additional information
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kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
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additional information
additional information
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the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
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additional information
additional information
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
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additional information
additional information
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kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
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additional information
additional information
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
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additional information
additional information
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
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additional information
additional information
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calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
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additional information
additional information
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
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additional information
additional information
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Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
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