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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession P0AGJ9

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Escherichia coli
UNIPROT: P0AGJ9 not found.
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
CHOTyrRS, class I tyrosyl-tRNA synthetase, CYT-18, CYT-18 protein, dTyRS, hTyrRS, LdTyrRS, LMJF_14_1370, mini-tyrosyl-tRNA synthetase, mini-TyrRS, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tyrosine translase
-
-
-
-
Tyrosine tRNA synthetase
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
-
Tyrosyl--tRNA ligase
-
-
-
-
Tyrosyl-transfer ribonucleate synthetase
-
-
-
-
Tyrosyl-transfer ribonucleic acid synthetase
-
-
-
-
Tyrosyl-transfer RNA synthetase
-
-
-
-
Tyrosyl-tRNA ligase
-
-
-
-
Tyrosyl-tRNA synthetase
TyrRS
tyrS
295446
gene name
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acylation
esterification
PATHWAY SOURCE
PATHWAYS
MetaCyc
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-tyrosine + tRNATyr
AMP + diphosphate + D-tyrosyl-tRNATyr
show the reaction diagram
-
enzyme TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
AMP + diphosphate
ATP
show the reaction diagram
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
show the reaction diagram
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
additional information
?
-
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
show the reaction diagram
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acacetin
-
strong inhibition
chrysin
-
strong inhibition
epigallocatechin gallate
-
strong inhibition
kaempferide
-
strong inhibition
AMP
-
inhibition is weakened by chloride
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
diphosphate
-
inhibition is strengthened by chloride
sulfate
-
inhibition in presence of 1 mM free Mg2+
tRNATyr
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043 - 0.00223
ATP
0.00669 - 0.00845
L-tyrosine
0.00037 - 0.00048
tRNATyr
0.13
3-iodo-L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.5
ATP
-
ATP-diphosphate exchange reaction
0.018 - 0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.0033 - 0.14
L-tyrosine
0.000022 - 0.00052
tRNATyr
0.008 - 0.012
tyrosine
0.0002
tyrosyl-tRNATyr
-
deacylation
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 14.2
ATP
0.1 - 14.2
L-tyrosine
0.15 - 1.32
tRNATyr
0.43
3-iodo-L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.042 - 0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.045 - 12
L-tyrosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
140 - 33020
ATP
10 - 1990
L-tyrosine
0.33 - 3.51
tRNATyr
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 0.9
AMP
0.056 - 0.14
diphosphate
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.8
-
assay at
7.4
-
assay at
7.5
-
assay at
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
TyrRS is a member of class I aminoacyl-tRNA synthetases
malfunction
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
2 * 47000, SDS-PAGE
90000
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sucrose density gradient centrifugation
97000
-
PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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-
dimer
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2 * 47000, SDS-PAGE
additional information
-
three-dimensional modeling of the Escherichia coli enzyme constructed on the basis of the X-ray crystal structure of Bacillus stearothermophilus enzyme complexed with tyrosinyl adenylate, PDB code 3TS1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
tyrosyl-tRNA synthetase (TyrRS) in Escherichia coli is acetylated at multiple lysine residues. Acetylation at K85, K235, and K238 impairs the enzyme activity, by genetic-code-expansion strategy to site-specifically incorporate Nepsilonacetyl-l-lysine into selected positions of TyrRS for in vitro characterization. Lysine residue K355 is never acetylated. Most acetylated lysine residues in TyrRS are sensitive to the Escherichia coli deacetylase CobB but not YcgC, overview. Mapping of acetylated lysine residues on the crystal structure of TyrRS, PDB ID 1VBM
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor-diffusion method. Crystal structures of TyrRS catalytic domain, in complex with L-tyrosine and L-tyrosyladenylate analogue, 5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine, are solved at 2.0 A and 2.7 A resolution
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the iodoTyrRS-ec-3-azide-L-tyrosine structure is determined at a resolution of 1.8 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D41N
-
site-directed mutagenesis
D81H/Q179E/Q201D
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site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81K/Q179E
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site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81K/Q179E/Q201D
-
site-directed mutagenesis, the mutant shows no activity for L-Tyr and D-Tyr
D81N
-
site-directed mutagenesis, the mutant shows a preference for L-Tyr that is much stronger than for the wild-type TyrRS. The ligand ammonium is coordinated at the L-Tyr endpoint by Asp41 (which replaces Asp81 in the coordination shell) and Tyr175 but not Gln179. At the D-Tyr endpoint, the ligand ammonium is coordinated by a mixture of Gln201, Tyr175, Asp41, and sometimes weakly by Gln179
D81R
-
site-drected mutagenesis, the mutant shows low activity for L-Tyr and D-Tyr, and the same KM value for L-Tyr compared to wild-type enzyme, the mutant is D-Tyr specific, but with low activity
F130S
-
construction of a plasmid library of randomly mutated gene tyrS by PCR, isolation of a mutant R-6-A-7 which incorporates L-beta-(5-hydroxy-2-pyridyl)-alanine in transformed Escherichia coli cells in vivo, increased temperature instability
Q179A
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179E
-
inactive mutant
Q179N
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179S
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179Y
-
inactive mutant
Q195A
-
site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195C
-
site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195D
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195E
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195F
-
inactive mutant
Q195G
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195H
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195I
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195K
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inactive mutant
Q195L
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195M
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195N
-
site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195R
-
inactive mutant
Q195S
-
site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195T
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195V
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195W
-
inactive mutant
Q195Y
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37A/Q195A
-
inactive mutant
Y37A/Q195C
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37A/Q195N
-
inactive mutant
Y37A/Q195S
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195A
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195C
-
inactive mutant
Y37I/Q195N
-
inactive mutant
Y37I/Q195S
-
inactive mutant
Y37L/Q195A
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195C
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37L/Q195N
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195S
-
inactive mutant
Y37V/Q195N
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37V/Q195S
-
site-directed mutagenesis, reduced activity with L-tyrosine and 3-iodo-L-tyrosine
Y73A
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73F
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y73G
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine, reduced overall activity
Y73H
-
site-directed mutagenesis, active with L-tyrosine, and slightly active with 3-iodo-L-tyrosine
Y73I
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter
Y73L
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73M
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73S
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the first
Y73V
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73V/Q195A
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y73V/Q195C
-
site-directed mutagenesis, 10fold more active with 3-iodo-L-tyrosine than with L-tyrosine, reduced overall activity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
-
40% loss of activity in 4-12 min, depending on the bacterial strains used for purification, stabilization by substrates
50
-
10 min, wild-type enzyme is not affected, while the mutant F130S is almost completely inactivated
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Tyrosine and/or ATP stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
-20°C, 0.025 M potassium phosphate buffer, pH 6.7, 0.01 M 2-mercaptoethanol, 50% glycerol, no loss of activity in 6 months
-
4°C, 20 mM Tris-HCl buffer, pH 7, 80% loss of activity within 48 h, 5% loss of activity in presence of 10% glycerol and 3 mM 2-mercaptoethanol
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity, recombinant His-tagged mutant enzymes from Saccharomyces cerevisiae strain BY4742 by nickel affinity chromatography to over 90% purity
-
recombinant His6-tagged wild-type enzyme and site-specifically acetylated TyrRS variants from Escherichia coli strain BL21(DE3) cells
-
catalytic domain (residues 1-322)
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3)
-
recombinant HIs-tagged wild-type and mutant F130S from strain JM109
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene tyrS, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged mutant enzymes in Saccharomyces cerevisiae strain BY4742
-
gene tyrS, recombinant expression of His6-tagged wild-type enzyme and site-specifically acetylated TyrRS variants in Escherichia coli strain BL21(DE3) cells
-
catalytic domain (residues 1-322)
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gene tyrS, expression of wild-type and mutant enzymes as His-tagged proteins in strain JM109
-
into the vectors pACYC184 and pAp102
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overexpression of His-tagged wild-type and mutants in strain BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lysine acetylation can be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
TyrRS enzymes are candidates for therapeutic targets in the prevention and therapy of microbial infections
biotechnology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
2
Grosse, F.; Krauss, G.; Kownatzki, R.; Maass, G.
The binding of tyrosinyl-5'-AMP to tyrosyl synthetase (E. coli)
Nucleic Acids Res.
6
1631-1638
1979
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
8
Chousterman, S.; Chapeville, F.
Tyrosyl-tRNA synthetase of Escherichia coli B. Role of magnesium in the reaction catalyzed by the enzyme
Eur. J. Biochem.
35
46-50
1988
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
Chousterman, S.; Chapeville, F.
Escherichia coli tyrosyl-tRNA synthetase. Influence of magnesium ions on the enzme activity
FEBS Lett.
17
153-157
1971
Escherichia coli
Manually annotated by BRENDA team
Buonocore, V.; Harris, M.H.; Schlesinger, S.
Properties of tyrosyl transfer ribonucleic acid synthetase from two tyrS mutants of Escherichia coli K-12
J. Biol. Chem.
247
843-4849
1972
Escherichia coli, Escherichia coli (P0AGJ9)
-
Manually annotated by BRENDA team
Chousterman, S.; Chapeville, F.
Tyrosyl-tRNA synthetase of Escherichia coli B
Eur. J. Biochem.
35
51-56
1973
Escherichia coli
Manually annotated by BRENDA team
Jakes, R.; Fersht, A.R.
Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and of half-of-the-sites reactivity in aminoacylation
Biochemistry
14
3344-3350
1975
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
Bruton, C.; Jakes, R.; Atkinson, T.
Gram-scale purification of methionyl-tRNA and tyrosyl-tRNA synthetases from Escherichia coli
Eur. J. Biochem.
59
327-333
1975
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
Airas, R.K.
Chloride affects the interaction between tyrosyl-tRNA synthetase and tRNA
Biochim. Biophys. Acta
1472
51-61
1999
Escherichia coli, Geobacillus stearothermophilus
Manually annotated by BRENDA team
Hamano-Takaku, F.; Iwama, T.; Saito-Yano, S.; Takaku, K.; Monden, Y.; Kitabatake, M.; Soll, D.; Nishimura, S.
A mutant Escherichia coli tyrosyl-tRNA synthetase utilizes the unnatural amino acid azatyrosine more efficiently than tyrosine
J. Biol. Chem.
275
40324-40328
2000
Escherichia coli
Manually annotated by BRENDA team
Kiga, D.; Sakamoto, K.; Kodama, K.; Kigawa, T.; Matsuda, T.; Yabuki, T.; Shirouzu, M.; Harada, Y.; Nakayama, H.; Takio, K.; Hasegawa, Y.; Endo, Y.; Hirao, I.; Yokoyama, S.
An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
Proc. Natl. Acad. Sci. USA
99
9715-9720
2002
Escherichia coli
Manually annotated by BRENDA team
Kobayashi, T.; Takimura, T.; Sekine, R.; Kelly, V.P.; Kamata, K.; Sakamoto, K.; Nishimura, S.; Yokoyama, S.
Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase
J. Mol. Biol.
346
105-117
2005
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
Iraha, F.; Oki, K.; Kobayashi, T.; Ohno, S.; Yokogawa, T.; Nishikawa, K.; Yokoyama, S.; Sakamoto, K.
Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion
Nucleic Acids Res.
38
3682-3691
2010
Escherichia coli, Escherichia coli (P0AGJ9), Methanocaldococcus jannaschii, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Venkat, S.; Gregory, C.; Gan, Q.; Fan, C.
Biochemical characterization of the lysine acetylation of tyrosyl-tRNA synthetase in Escherichia coli
ChemBioChem
18
1928-1934
2017
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
Skupinska, M.; Stepniak, P.; Letowska, I.; Rychlewski, L.; Barciszewska, M.; Barciszewski, J.; Giel-Pietraszuk, M.
Natural compounds as inhibitors of tyrosyl-tRNA synthetase
Microb. Drug Resist.
23
308-320
2017
Escherichia coli, Escherichia coli (P0AGJ9), Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HWP3), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HWP3), Staphylococcus aureus
Manually annotated by BRENDA team
Simonson, T.; Ye-Lehmann, S.; Palmai, Z.; Amara, N.; Wydau-Dematteis, S.; Bigan, E.; Druart, K.; Moch, C.; Plateau, P.
Redesigning the stereospecificity of tyrosyl-tRNA synthetase
Proteins
84
240-253
2016
Escherichia coli, Escherichia coli (P0AGJ9)
Manually annotated by BRENDA team
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