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Literature summary for 6.1.1.1 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene tyrZ, overexpression of the HIs-tagged enzyme in Escherichia coli strain JM105 | Acidithiobacillus ferrooxidans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H306A | no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 3fold decrease in kcat for amino acid activation | Acidithiobacillus ferrooxidans |
| H306D | no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109 | Acidithiobacillus ferrooxidans |
| H53A | no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, inactive | Acidithiobacillus ferrooxidans |
| K395N | slight complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 17fold increase in Km for Escherichia coli tRNATyr, reduced activity | Acidithiobacillus ferrooxidans |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | mutants | Acidithiobacillus ferrooxidans | |
| 0.0025 | - |
tRNATyr | aminoacylation reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans |  |
| 0.021 | - |
L-tyrosine | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 0.027 | - |
L-tyrosine | aminoacylation reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 0.07 | - |
ATP | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 0.13 | - |
ATP | aminoacylation reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Acidithiobacillus ferrooxidans | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48000 | - |
2 * 48000, recombinant His-tagged enzyme, SDS-PAGE | Acidithiobacillus ferrooxidans |
| 105000 | - |
recombinant His-tagged enzyme, gel filtration | Acidithiobacillus ferrooxidans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + tyrosine + tRNATyr | Acidithiobacillus ferrooxidans | - |
AMP + Tyr-tRNATyr + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidithiobacillus ferrooxidans | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant HIs-tagged enzyme from overexpression in Escherichia coli strain JM105 | Acidithiobacillus ferrooxidans |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Acidithiobacillus ferrooxidans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + tyrosine + tRNATyr | - |
Acidithiobacillus ferrooxidans | AMP + Tyr-tRNATyr + diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 48000, recombinant His-tagged enzyme, SDS-PAGE | Acidithiobacillus ferrooxidans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tyrosine tRNA synthetase | - |
Acidithiobacillus ferrooxidans |
| TyrRZ | - |
Acidithiobacillus ferrooxidans |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | mutants | Acidithiobacillus ferrooxidans | |
| 3.3 | - |
ATP | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 3.3 | - |
L-tyrosine | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 5.29 | - |
ATP | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 5.29 | - |
L-tyrosine | phosphate exchange reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 7.7 | - |
ATP | aminoacylation reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
| 7.7 | - |
L-tyrosine | aminoacylation reaction, pH 8.0, wild-type enzyme | Acidithiobacillus ferrooxidans | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Acidithiobacillus ferrooxidans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Acidithiobacillus ferrooxidans | |
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