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Literature summary for 6.1.1.1 extracted from

  • Xin, Y.; Li, W.; First, E.A.
    Stabilization of the transition state for the transfer of tyrosine to tRNATyr by tyrosyl-tRNA synthetase (2000), J. Mol. Biol., 303, 299-310.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutants into the phagemid pYTS5-WT Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
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 Geobacillus stearothermophilus
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 Geobacillus stearothermophilus
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 Geobacillus stearothermophilus
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 Geobacillus stearothermophilus
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 Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information 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 Geobacillus stearothermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + tyrosine + tRNATyr Geobacillus stearothermophilus
-
AMP + Tyr-tRNATyr + diphosphate
-
r

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr mechanism, residues Asp78, Tyr169, Gln173, Asp194, and Gln195 are involved in catalysis Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + tyrosine + tRNATyr
-
Geobacillus stearothermophilus AMP + Tyr-tRNATyr + diphosphate
-
r
ATP + tyrosine + tRNATyr 2-step reaction: 1. tyrosine activation to form the tyrosinyl-adenylate intermediate, 2. transfer of tyrosine from the tyrosinyl-adenylate intermediate to the tRNATyr Geobacillus stearothermophilus AMP + Tyr-tRNATyr + diphosphate
-
r

Synonyms

Synonyms Comment Organism
Tyrosyl-tRNA synthetase
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Geobacillus stearothermophilus