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Literature summary extracted from

  • Salazar, J.C.; Zuniga, R.; Lefimil, C.; Soll, D.; Orellana, O.
    Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding (2001), FEBS Lett., 491, 257-260.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.1 gene tyrZ, overexpression of the HIs-tagged enzyme in Escherichia coli strain JM105 Acidithiobacillus ferrooxidans

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.1 H306A no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 3fold decrease in kcat for amino acid activation Acidithiobacillus ferrooxidans
6.1.1.1 H306D no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109 Acidithiobacillus ferrooxidans
6.1.1.1 H53A no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, inactive Acidithiobacillus ferrooxidans
6.1.1.1 K395N slight complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 17fold increase in Km for Escherichia coli tRNATyr, reduced activity Acidithiobacillus ferrooxidans
6.1.1.1 S356A no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 7fold increase in Km for Escherichia coli tRNATyr, reduced activity Acidithiobacillus ferrooxidans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.1 additional information
-
 additional information mutants Acidithiobacillus ferrooxidans
6.1.1.1 0.0025
-
 tRNATyr aminoacylation reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 0.021
-
 L-tyrosine phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 0.027
-
 L-tyrosine aminoacylation reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 0.07
-
 ATP phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 0.13
-
 ATP aminoacylation reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.1 Mg2+ required Acidithiobacillus ferrooxidans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.1 48000
-
 2 * 48000, recombinant His-tagged enzyme, SDS-PAGE Acidithiobacillus ferrooxidans
6.1.1.1 105000
-
 recombinant His-tagged enzyme, gel filtration Acidithiobacillus ferrooxidans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.1 ATP + tyrosine + tRNATyr Acidithiobacillus ferrooxidans
-
 AMP + Tyr-tRNATyr + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.1 Acidithiobacillus ferrooxidans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.1 recombinant HIs-tagged enzyme from overexpression in Escherichia coli strain JM105 Acidithiobacillus ferrooxidans

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.1 ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr S356 and K395 play key roles in tRNA binding, H306, a residue at the junction of the catalytic and tRNA binding domains, stabilizes the Tyr-AMP:enzyme complex Acidithiobacillus ferrooxidans
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1.1.1 additional information
-
-
 Acidithiobacillus ferrooxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.1 ATP + tyrosine + tRNATyr
-
 Acidithiobacillus ferrooxidans AMP + Tyr-tRNATyr + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.1 dimer 2 * 48000, recombinant His-tagged enzyme, SDS-PAGE Acidithiobacillus ferrooxidans

Synonyms

EC Number Synonyms Comment Organism
6.1.1.1 Tyrosine tRNA synthetase
-
 Acidithiobacillus ferrooxidans
6.1.1.1 TyrRZ
-
 Acidithiobacillus ferrooxidans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.1 additional information
-
 additional information mutants Acidithiobacillus ferrooxidans
6.1.1.1 3.3
-
 ATP phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 3.3
-
 L-tyrosine phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 5.29
-
 ATP phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 5.29
-
 L-tyrosine phosphate exchange reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 7.7
-
 ATP aminoacylation reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans
6.1.1.1 7.7
-
 L-tyrosine aminoacylation reaction, pH 8.0, wild-type enzyme Acidithiobacillus ferrooxidans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.1 8
-
 assay at Acidithiobacillus ferrooxidans

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.1 ATP
-
 Acidithiobacillus ferrooxidans