Information on EC 6.1.1.1 - tyrosine-tRNA ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.1.1.1
-
RECOMMENDED NAME
GeneOntology No.
tyrosine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
tRNA charging
-
-
tyrosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeropyrum pernix DSM 11879
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain HB27, purified recombinant enzyme
-
-
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
phylogenetic relationship of TyrRS sequences, schematic overview
physiological function
additional information
-
dissociating quaternary structures regulating novel functions of other tRNA synthetases
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + diphosphate
ATP
show the reaction diagram
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
show the reaction diagram
ATP + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
?
show the reaction diagram
-
-
-
-
?
ATP + 3-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
show the reaction diagram
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
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 + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
show the reaction diagram
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
show the reaction diagram
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
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 + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
show the reaction diagram
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
show the reaction diagram
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + p-acetyl-L-phenylalanine + tRNATyr
AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
show the reaction diagram
-
aminoacyl-tRNA synthetases are designed through a combination of homology modeling, molecular docking and binding affinity computation with the purpose of incorporating pACPhe into proteins in Escherichia coli
-
-
?
ATP + p-iodophenylalanine + tRNATyr
AMP + diphosphate + p-iodophenylalanyl-tRNATyr
show the reaction diagram
-
a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
-
-
?
ATP + tyrosine + tRNATyr
?
show the reaction diagram
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
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
?
show the reaction diagram
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
replacement of the morpholine-ring in the side chain of the compound with a substituent containing more hydrophilic groups is probably more suitable for further modification. Most potent agent against Staphylococcus aureus ATCC 25923 with MIC50 value of 0.00023 mg/ml
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
-
-
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2,4-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-chlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2-methylphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3,4-dichlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3,4-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3,4-dimethoxyphenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3,5-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(3-chlorophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(3-trifluoromethylphenylformyoxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(4-bromophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(4-chlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(4-fluorophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-fluorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
-
4-(2-(4-hydroxyphenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-methylphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(6-hydroxynaphthalen-2-ylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(naphthalen-2-ylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
-
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
-
-
-
6-Aminomethyladenosine triphosphate
-
-
chloride
diphosphate
fisetin
-
binding structure, overview
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl N6-benzoyl adenylate
-
-
L-tyrosinyl uridine-5'-O-phosphate
L-tyrosinyl-2',3'-O-isopropylidene adenylate
L-tyrosinyl-2'-deoxy adenylate
L-tyrosinyl-3'-deoxy adenylate
N-ethylmaleimide
-
-
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
sulfate
tRNATyr
-
-
tyrosinol
-
binding structure, overview
tyrosinyl adenylate
tyrosyl aryl dipeptides
-
inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.04 - 2.43
3-chloro-L-tyrosine
0.625 - 1.3
3-fluoro-D,L-tyrosine
0.13 - 1.15
3-iodo-L-tyrosine
1.6
A22G mutated tRNATyr transcript
-
-
-
0.04 - 7
ATP
0.46 - 14
D-tyrosine
0.8
G15A mutated tRNATyr transcript
-
-
-
22 - 32
K+
0.56 - 1.84
L-3,4-dihydroxyphenylalanine
0.018 - 0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.0003 - 1.19
L-tyrosine
0.002
native yeast tRNATyr
-
pH 7.5, 30C
-
0.000022 - 4.8
tRNATyr
0.00068 - 0.039
tRNATyr(G34C)
0.00035 - 0.0014
tRNATyr(wild-type)
0.0015
tRNYTyr
-
-
-
0.002 - 0.013
tyrosine
0.0002
tyrosyl-tRNATyr
-
deacylation
-
2.2
U54C mutated tRNATyr transcript
-
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 6.08
3-chloro-L-tyrosine
0.62 - 6.08
3-fluoro-D,L-tyrosine
0.43 - 0.48
3-iodo-L-tyrosine
0.00003
A22G mutated tRNATyr transcript
Homo sapiens
-
-
-
3.3 - 12
ATP
0.37 - 1.2
D-tyrosine
0.0002
G15A mutated tRNATyr transcript
Homo sapiens
-
-
-
0.67 - 6.08
L-3,4-dihydroxyphenylalanine
0.042 - 0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.01 - 45
L-tyrosine
1.5
native yeast tRNATyr
Saccharomyces cerevisiae
-
pH 7.5, 30C
-
0.046 - 6.08
tRNATyr
0.07 - 0.079
tRNATyr(G34C)
0.12 - 0.19
tRNATyr(wild-type)
0.012
U54C mutated tRNATyr transcript
Homo sapiens
-
-
-
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300 - 1318
tRNATyr
additional information
additional information
Aeropyrum pernix
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32 - 2.15
AMP
0.048 - 0.23
diphosphate
0.076 - 0.42
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
0.0057 - 0.15
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
0.000011
L-tyrosinyl adenylate
-
pH 7.9, 37C
0.00068
L-tyrosinyl N6-benzoyl adenylate
-
pH 7.9, 37C
0.00021
L-tyrosinyl uridine-5'-O-phosphate
-
pH 7.9, 37C
0.0000093 - 0.000026
L-tyrosinyl-2',3'-O-isopropylidene adenylate
0.018 - 0.1
L-tyrosinyl-2'-deoxy adenylate
0.036 - 0.14
L-tyrosinyl-3'-deoxy adenylate
0.0000063
tyrosinyl adenylate
-
pH 7.9, 37C
additional information
additional information
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
0.0243
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0205
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0256
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0375
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00062
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0328
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0536
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0291
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0355
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0165
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0502
4-(2-(2,4-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0052
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0568
4-(2-(2-chlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0414
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0647
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(2-methylphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0182
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0334
4-(2-(3,4-dichlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0753
4-(2-(3,4-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0838
4-(2-(3,4-dimethoxyphenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0067
4-(2-(3,5-dihydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0035
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0011
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(3-chlorophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0009
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.081
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.026
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0043
4-(2-(3-trifluoromethylphenylformyoxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0167
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0481
4-(2-(4-bromophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0093
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0088
4-(2-(4-chlorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0057
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0936
4-(2-(4-fluorophenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0075
4-(2-(4-fluorophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0079
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(4-hydroxyphenylacetyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0112
4-(2-(4-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0178
4-(2-(4-methylphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0086
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0052
4-(2-(4-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0168
4-(2-(6-hydroxynaphthalen-2-ylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.1
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0719
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.1
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0874
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0177
4-(2-(naphthalen-2-ylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0846
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0478
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0062
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.041
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
0.0128
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000076
-
purified recombinant His-tagged enzyme
1.8
-
purified enzyme
18.35
-
-
1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
-
aminoacylation
1
7.5 - 9
-
-
7.5 - 9
-
ATP-diphosphate exchange reaction
1
7.7 - 8
-
kinetic assays
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
1
7.2 - 8.5
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
aminoacylation assay at room temperature
55
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
a model is proposed, in which the KMSKS signature sequence is conformationally constrained and unable to participate in catalysis below 25C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lung cancer giant-cell strain
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
bovine aortic endothelial cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
mini-TyrRS is reduced in extracts of ischemic calf muscle and in thoracic aorta explants exposed to hypoxia or VEGF
Manually annotated by BRENDA team
-
differentiating, YARS locates mostly in the granular structures of the growth cone, branch points and the most distal part of of projecting neurites, co-localization with synaptophysin
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
YARS is expressed ubiquitously, in neuronal cells making extensions, the enzyme is located at outgrowth behaving like an early polarity maker, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
axonal termini in differentiating primary motor neuron and neuroblastoma cultures
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Coccidioides posadasii (strain C735)
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
calculation from sequence of tyrZ gene
38800 - 40300
-
sedimentation equilibrium centrifugation
43000 - 46500
-
sedimentation equilibrium centrifugation
43000
-
Western blot
50000
-
synthetase T1, gel filtration
70000
-
synthetase T2, gel filtration
90000
-
sucrose density gradient centrifugation
95000
-
gel filtration
97000
-
PAGE
100000
-
gel filtration
105000
-
recombinant His-tagged enzyme, gel filtration
110000
-
gel filtration
120000
-
gel filtration
130000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 40000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the C-terminal domain of the enzyme, which has cytokine and angiogenic activity and stimulates immune cells, is isolated by proteolytic cleavage or alternative splicing, the mini enzyme is a stimulator of blood vessel development, the full-length enzyme is inactive
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified selenomethionyl-TyrRSapm in complex with tyrosinol, crystallization is improved by introducing anion-exchange chromatography, vapour diffusion method, 0.002 ml of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.4, 25C, is mixed with 500 nl reservoir solution containing 0.1 M sodium citrate, pH 5.5, and 6-9% PEG 4000 w/v, 15% 2-methyl-2,4-pentane-d12-diol, 0.1 M KCl, 1 mM MgCl2, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
crystal of SeMet-substituted TyrRS is obtained by the microbatch method, using an automatic crystallization robot. The crystals are grown at 20C in a month. The crystal of native TyrRS is obtained by hanging-drop, vapor-diffusion method. Crystals of SeMet-substituted TyrRS belong to the space group P4(3)2(1)2, with unit cell parameters a = b = 66.66 A, c = 197.48 A. Crystals of native TyrRS belong to the space group P4(3)2(1)2 with unit cell parameters a = b = 65.91 A, c = 196.17 A
-
hanging-drop vapour-diffusion method, The crystals belong to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 66.1, c= 196.2 A, and diffract to beyond 2.15 A resolution
-
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1), with unit cell parameters a = 40.62 A, b = 96.16 A, c = 92.64 A, beta = 94.41
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
-
the iodoTyrRS-ec-3-azide-L-tyrosine structure is determined at a resolution of 1.8 A
-
electron density map, X-ray structure
-
3
quarternary structure
-
4
T51 mutants of tyrosyl-tRNA synthetase
X-ray diffraction, at 2.7 A resolution, structure analysis of the enzyme-ligand complex, e.g. with specific synthetic inhibitors, molecular modeling
-
mutant mt-TyrRS-DS4, lacking the C-terminal S4-like domain, in complex with Tyr-AMS, an adenylate analogue, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
-
purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20C or 4C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
sitting-drop vapor-diffusion method. Space group P2(1)2(1)2(1) with two molecules per asymmetric unit, with unit cell dimensions a = 45.12 A, b = 185.29 A, and c = 95.48 A. Crystal structures for the apo wild-type and O-methyl-L-tyrosine-specific mutant enzyme are determined at 2.66 A and 3.0 A
-
structure of the TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A
-
hanging-drop vapour diffusion method. The crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 49.2 A, b = 156.5 A, c = 55.2 A, beta = 94.2
-
1.95 A crystal structure of mutant DELTA424-669 of CYT-18 protein. DELTA424-669 crystals are grown by sitting-drop vapor diffusion. The crystals are in space group C2 with unit cell dimensions: a = 104.88 A, b = 73.21 A, c = 56.79 A, beta = 111.35
-
a 4.5 A co-crystal structure of the Twort orf 142-I2 group I intron ribozyme bound to splicing-active, carboxy-terminally truncated CYT-18. Structure shows that the group I intron binds across the two subunits of the homodimeric protein with a newly evolved RNA-binding surface distinct from that which binds tRNATyr. This RNA binding surface provides an extended scaffold for the phosphodiester backbone of the conserved catalytic core of the intron RNA, allowing the protein to promote the splicing of a wide variety of group I introns. The group I intron-binding surface includes three small insertions and additional structural adaptations relative to non-splicing bacterial TyrRSs, indicating a multistep adaptation for splicing function
-
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 74.35 A, b = 88.26 A, c = 162.92 A
crystal structure at 2.3 A resolution
-
purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution
crystal structure determination by X-ray diffraction, enzyme complexed with inhibitors at 2.8 A resolution, and truncated enzyme complexed with inhibitors at 2.2 A resolution
-
enzyme complexed to a tyrosyl aryl dipeptide inhibitor, structure analysis
-
pure enzyme, 12 mg/ml, or in complex with tyrosinol, hanging drop vapour diffusion technique, equal volumes of protein and a reservoir solution that contains 1.2 M ammonium sulfate, 10 mM MgCl2, 0.5 mM dithiothreitol, 50 mM MES, pH 5.8, X-ray diffraction structure determination and analysis, enzyme in complex with tyrosinol, ATP and tRNATyr, at 293K, equilibration of 0.004 ml protein-RNA solution against 1 ml reservoir solution, protein-RNA solution: 4-5 mg/ml of enzyme in a molar ratio of 1:1 or 1:2 with RNA, 5 mM tyrosinol, 10 mg MgCl2, 10 mM ATP, 50 mM HEPES, pH 7.0, 0.8 M ammonium sulfate, reservoir solution: 1.5-1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, 2-4 weeks, X-ray diffraction structure determination at 2.0-2.1 A resolution and analysis
-
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
68.5
-
wild-type enzyme shows 50% inactivation after 27 min
additional information
-
effects of mutations and of coupling of mutations on thermal parameters and stability, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution has denaturing effect
-
stable to immediate freezing and thawing, but not for longer periods, no stabilization by potassium borohydrite, MgCl2, ATP, Vitamin B12
-
Tyrosine and/or ATP stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, rapid loss of activity, 0.05 M GSH plus 0.005 M EDTA stabilizes
-
-20C, 0.025 M potassium phosphate buffer, pH 6.7, 0.01 M 2-mercaptoethanol, 50% glycerol, no loss of activity in 6 months
-
-20C, 4 months stable
-
4C, 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
by ammonium sulfate precipitation and on a heparin-Sepharose column
-
by chromatography on Ni-nitrilotriacetic acid agarose
-
by utilizing the His-tag
-
catalytic domain (residues 1-322)
-
Cibacron Blue 3GA column chromatography
-
mutant DELTA424-669
-
on a Source 15Q-Sepharose anion-exchange column
-
recombinant C-terminal domain from Escherichia coli strain BL21(DE3) by cation exchange chromatography and gel filtration
-
recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase from Escherichia coli by nickel affinity and ion exchange chromatography to homogeneity
-
recombinant enzyme to near homogeneity
-
recombinant His-Tagged enzyme form Escherichia coli strain BL21(DE3), removal of the N-terminal His-tag
-
recombinant His-tagged enzyme from Escherichia coli strain BL21, 4.2fold
-
recombinant HIs-tagged enzyme from overexpression in Escherichia coli strain JM105
-
recombinant His-tagged full-length wild-type and mutant mitochondrial enzymes, and truncated mutant mt-TyrRS-DS4 mitochondrial enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3)
-
recombinant HIs-tagged wild-type and mutant F130S from strain JM109
-
recombinant His-tagged wild-type and mutant Y43G enzyme from Escherichia coli Y43G
-
recombinant truncated enzyme SceTyrRS comprising residues 1-364
recombinant TyrRSfrom Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant wild-type and mutant His-tagged enzymes
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synthetase 1-3
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synthetase T1 and T2
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using Ni-NTA chromatography
wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a library of more than 200 mutants substituting the ATP binding motif KMSSS, Lys204-Met205-Ser206-Ser207-Ser208, is built, mutants and wild-type of MjYRS are cloned into the vector pET41a+
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catalytic domain (residues 1-322)
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CYT-18 is expressed from the plasmid pEX560 in the Escherichia coli strain HMS174DE3
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DNA and amino acid sequence determination and analysis of two enzymes types, expression of tyrosyl aminoacyl-tRNA synthetase as C-terminally His6-tagged enzyme in Escherichia coli
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DNA and amino acid sequence determination of wild-type and mutant enzymes, localization of the gene encoding the enzyme on chromosome 1p34-p35, functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, overview, transient expression of EGFP-tagged wild-type and mutant enzymes in murine neuroblastoma N2a cells
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expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells; expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli strain BL21(DE3)
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expression of C-terminal domain of TyrRS in Escherichia coli strain BL21(DE3)
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expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli
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expression of the enzyme as His-tagged protein in Escherichia coli strain BL21(DE3)
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expression of truncated enzyme SceTyrRS comprising residues 1-364
expression of wild-type and mutant enzymes as His-tagged proteins in Escherichia coli
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for expression in Escherichia coli TG2 cells
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gene structure and motifs in double-length TyrRS homologues, phylogenetic comparison
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gene TyrS, DNA sequence determination, overexpression as His-tagged enzyme in Escherichia coli BL21
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gene tyrS, expression of wild-type and mutant enzymes as His-tagged proteins in strain JM109
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gene tyrS, overexpression of wild-type and mutant enzymes from phage M13-BY(DELTA1) in Escherichia coli strains RZ1032 and TG2
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gene tyrZ, overexpression of the HIs-tagged enzyme in Escherichia coli strain JM105
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into the pUAST transformation vector
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into the single copy plasmid YCplac111
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into the TOPO TA cloning vector for sequencing
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into the vectors pACYC184 and pAp102
mutant human mini-TyrRS constructs are generated using QuikChange site-directed mutagenesis kit and using a plasmid encoding the gene for wild-type human mini-TyrRS as the template for PCR mutagenesis reactions, all proteins are expressed with a C-terminal His-tag to facilitate purification
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overexpression in Escherichia coli
overexpression of His-tagged wild-type and mutant Y43G enzyme in Escherichia coli BL21(DE3)
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overexpression of His-tagged wild-type and mutants in strain BL21(DE3)
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TyrRS, phylogenetic analysis, the viral aminoacyl tRNA synthetases have not been acquired recently by horizontal gene transfer from a cellular host but rather militate in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes
wild-type and mutants into the phagemid pYTS5-WT
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose significantly decreases mRNA expression of tyrosyl-tRNA synthetase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H306A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 3fold decrease in kcat for amino acid activation
H306D
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109
H53A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, inactive
K395N
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slight complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 17fold increase in Km for Escherichia coli tRNATyr, reduced activity
S356A
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no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 7fold increase in Km for Escherichia coli tRNATyr, reduced activity
D172H
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mutant enzyme shows a significant reductions in tyrosylation activity
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