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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P00952

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Geobacillus stearothermophilus
UNIPROT: P00952 not found.
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, cyt-18 protein, tyrosyl trna synthetase, mttyrrs, ldtyrrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tyrosyl-tRNA synthetase
-
Tyrosine translase
-
-
-
-
Tyrosine tRNA synthetase
-
-
-
-
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
-
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
TyrRS
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
esterification
Acylation
PATHWAY SOURCE
PATHWAYS
-
-
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 + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
?
AMP + diphosphate
ATP
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
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-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
-
25% inhibition at 0.1 mM
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
-
L-tyrosinyl-2'-deoxy adenylate
-
-
L-tyrosinyl-3'-deoxy adenylate
-
-
sulfate
-
inhibition in presence of 1 mM free Mg2+
tyrosinyl adenylate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 2.7
ATP
0.0014 - 0.0021
L-tyrosine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6 - 12
ATP
2.5 - 5.4
L-tyrosine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32 - 2.15
AMP
0.048 - 0.23
diphosphate
0.076
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37°C
0.0057
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37°C
0.00068
L-tyrosinyl N6-benzoyl adenylate
-
pH 7.9, 37°C
0.0000093
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
pH 7.9, 37°C
0.018
L-tyrosinyl-2'-deoxy adenylate
-
pH 7.9, 37°C
0.036
L-tyrosinyl-3'-deoxy adenylate
-
pH 7.9, 37°C
0.0000063
tyrosinyl adenylate
-
pH 7.9, 37°C
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.8
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 8
-
kinetic assays
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYY_GEOSE
419
0
47303
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
T51 mutants of tyrosyl-tRNA synthetase
electron density map, X-ray structure
-
3
quarternary structure
-
4
X-ray diffraction, at 2.7 A resolution, structure analysis of the enzyme-ligand complex, e.g. with specific synthetic inhibitors, molecular modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T51A
the mutant demonstrates an increase in activity
T51G
the mutant demonstrates an increase in activity
T51P
the mutant demonstrates a 25fold increase in activity compared to the wild type enzyme
T51S
the mutant demonstrates an increase in activity
C35G
-
crystal structure of mutants Cys to Gly35 and Tyr to Phe34
D194A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
D78A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
I52L
-
unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, compensates mutation L105V partially, destabilized association between subunits
K233A
-
mutant shows a reduced affinity for ATP
L105V
-
unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, destabilization of the monomeric intermediate of unfolding, mutation can be partially compensated by mutation I52L
M55L
-
increase in kinetic stability at 68.5°C compared to the wild-type, mutation is not coupled to others in its effects, slightly increased kinetic stability at 68.5°C
Q173A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it destabilizes the transition state complex for the second reaction step
Q195A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
T234A
-
decrease of the forward rate constant by 540fold, 3fold increase in affinity of the enzyme for ATP
T34F
-
crystal structure of mutants Cys to Gly35 and Tyr to Phe34
T51P
-
increased enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5°C compared to the wild-type, slightly destalized mutant
Y169A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on a Source 15Q-Sepharose anion-exchange column
-
wild-type and mutant enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for expression in Escherichia coli TG2 cells
-
gene tyrS, overexpression of wild-type and mutant enzymes from phage M13-BY(DELTA1) in Escherichia coli strains RZ1032 and TG2
-
wild-type and mutants into the phagemid pYTS5-WT
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
enzyme inhibitors can be used as antibacterial agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
3
Bhat, T.N.; Blow, D.M.; Brick, P.
Tyrosyl-tRNA synthetase forms a mononucleotide-binding old
J. Mol. Biol.
158
699-709
1982
Geobacillus stearothermophilus
Manually annotated by BRENDA team
4
Jones, D.H.; McMillan, A.J.; Fersht, A.R.
Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface
Biochemistry
24
5852-5857
1985
Geobacillus stearothermophilus
Manually annotated by BRENDA team
5
Brown, K.A.; Vrielink, A.; Blow, D.M.
Crystal structure of two factitious mutants of tyrosyl-tRNA synthetase
Biochem. Soc. Trans.
14
1228-1229
1985
Geobacillus stearothermophilus
-
Manually annotated by BRENDA team
6
Ward, W.H.J.; Fersht, A.R.
Asymmetry of tyrosyl-tRNA synthetase in solution
Biochemistry
27
1041-1049
1988
Geobacillus stearothermophilus
Manually annotated by BRENDA team
7
Ward, W.H.J.; Fersht, A.R.
Tyrosyl-tRNA synthetase acts as an asymetric dimer in charging tRNA. A rationale for half-of-the-sites activity
Biochemistry
27
5525-5530
1988
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Reid, B.R.; Koch, G.L.E.; Boulanger, Y.; Hartley, B.S.; Blow, D.M.
Crystallization and preliminary X-ray diffraction studies on tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus
J. Mol. Biol.
80
199-201
1973
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Avis, J.M.; Day, A.G.; Garcia, G.A.; Fersht, A.R.
Reaction of modified and unmodified tRNATyr substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
Biochemistry
32
5312-5320
1993
Geobacillus stearothermophilus
Manually annotated by BRENDA team
First, E.A.; Fersht, A.R.
Involvement of threonine 234 in catalysis of threonyl adenylate formation by tyrosyl-tRNA synthetase
Biochemistry
32
13644-13650
1993
Geobacillus stearothermophilus
Manually annotated by BRENDA team
First, E.A.; Fersht, A.R.
Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase
Biochemistry
32
13651-13657
1993
Geobacillus stearothermophilus
Manually annotated by BRENDA team
First, E.A.; Fersht, A.R.
Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase
Biochemistry
32
13658-13663
1993
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Wells, T.N.C.; Knill-Jones, J.W.; Gray, T.E.; Fersht, A.R.
Kinetic and thermodynamic properties of wild-type and engineered mutants of tyrosyl-tRNA synthetase analyzed by pyrophosphate exchange kinetics
Biochemistry
30
5151-5156
1991
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Fothergill, M.D.; Fersht, A.R.
Correlations between kinetics and X-ray analyses of engineered enzymes - crystal structures of mutants Cys-->Gly35 and Tyr-->Phe34 of tyrosyl-tRNA synthetase
Biochemistry
30
5157-5164
1991
Geobacillus stearothermophilus
Manually annotated by BRENDA team
First, E.; Fersht, A.R.
Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
Biochemistry
34
5030-5043
1995
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Garcia, G.A.; Leatherbarrow, R.J.; Eckstein, F.; Fersht, A.R.
Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction
Biochemistry
29
1643-1648
1990
Geobacillus stearothermophilus
Manually annotated by BRENDA team
De Prat, G.; Duckworth, H.W.; Fersht, A.R.
Modification of amino acid specificity of tyrosyl-tRNA synthetase by protein engineering
FEBS Lett.
318
167-171
1993
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Koch, G.L.E.
Tyrosyl transfer ribonucleic acid synthetase from Bacillus stearothermophilus. Preparation and properties of the crystallizable enzyme
Biochemistry
13
2307-2312
1974
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Irwin, M.J.; Nyborg, J.; Reid, B.R.; Blow, D.M.
The crystal structure of tyrosyl-transfer RNA synthetase at 2.7 A resolution
J. Mol. Biol.
105
577-586
1976
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Monteilhet, C.; Blow, D.M.
Binding of tyrosine, adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetase
J. Mol. Biol.
122
407-417
1978
Geobacillus stearothermophilus
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
Geobacillus stearothermophilus, Escherichia coli
Manually annotated by BRENDA team
Brown, P.; Richardson, C.M.; Mensah, L.M.; O'Hanlon, P.J.; Osborne, N.F.; Pope, A.J.; Walker, G.
Molecular recognition of tyrosinyl adenylate analogues by prokaryotic tyrosyl tRNA synthetases
Bioorg. Med. Chem.
7
2473-2485
1999
Geobacillus stearothermophilus, Staphylococcus aureus
Manually annotated by BRENDA team
Park, Y.C.; Bedouelle, H.
Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions
J. Biol. Chem.
273
18052-18059
1998
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Austin, J.; First, E.A.
Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases
J. Biol. Chem.
277
28394-28399
2002
Geobacillus stearothermophilus, Homo sapiens
Manually annotated by BRENDA team
Xin, Y.; Li, W.; First, E.A.
Stabilization of the transition state for the transfer of tyrosine to tRNATyr by tyrosyl-tRNA synthetase
J. Mol. Biol.
303
299-310
2000
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Sharma, G.; First, E.
Thermodynamic analysis reveals a temperature-dependent change in the catalytic mechanism of Bacillus stearothermophilus tyrosyl-tRNA synthetase
J. Biol. Chem.
284
4179-4190
2009
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Brown, K.
A brief perspective of the determination of crystal structures of site-directed mutants of tyrosyl-tRNA synthetase
Protein Eng.
24
229-231
2011
Geobacillus stearothermophilus (P00952)
Manually annotated by BRENDA team