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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
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ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
AMP + diphosphate
ATP
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
Na2ATP2-, specific for tyrosine as amino acid
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
phosphorothioate analogs of ATP
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction: 1. tyrosine activation to form the tyrosinyl-adenylate intermediate, 2. transfer of tyrosine from the tyrosinyl-adenylate intermediate to the tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr substrate from Escherichia coli
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
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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
-
altered specificity for amino acid
additional information
-
kinetic properties ATP-diphosphate exchange reacion of engineered mutants
additional information
-
effects of coupling of mutations on thermal stability
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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
brenda
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
brenda
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
-
brenda
Ward, W.H.J.; Fersht, A.R.
Asymmetry of tyrosyl-tRNA synthetase in solution
Biochemistry
27
1041-1049
1988
Geobacillus stearothermophilus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Airas, R.K.
Chloride affects the interaction between tyrosyl-tRNA synthetase and tRNA
Biochim. Biophys. Acta
1472
51-61
1999
Geobacillus stearothermophilus, Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda