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Literature summary for 6.1.1.1 extracted from

  • Sharma, G.; First, E.
    Thermodynamic analysis reveals a temperature-dependent change in the catalytic mechanism of Bacillus stearothermophilus tyrosyl-tRNA synthetase (2009), J. Biol. Chem., 284, 4179-4190.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
for expression in Escherichia coli TG2 cells Geobacillus stearothermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on a Source 15Q-Sepharose anion-exchange column Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tyrosine + tRNATyr
-
 Geobacillus stearothermophilus AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?

Synonyms

Synonyms Comment Organism
Tyrosyl-tRNA synthetase
-
 Geobacillus stearothermophilus
TyrRS
-
 Geobacillus stearothermophilus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25
-
 a model is proposed, in which the KMSKS signature sequence is conformationally constrained and unable to participate in catalysis below 25°C Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7 8 kinetic assays Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Geobacillus stearothermophilus