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Literature summary for 6.1.1.19 extracted from
- An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions (2011), J. Biol. Chem., 286, 3396-3404.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of GST-tagged MtArgRS in Escherichia coli strain BL21(DE3), co-expression of MtArgRS with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, from in the Saccharomyces cerevisiae two-hybrid system using yeast strain MaV203 | Methanothermobacter thermautotrophicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview | Methanothermobacter thermautotrophicus | |
| 0.00466 | - |
tRNAArg | pH 7.5, 50°C, recombinant MtArgRS | Methanothermobacter thermautotrophicus |  |
| 0.00477 | - |
tRNAArg | pH 7.5, 50°C, recombinant MtArgRS in presence of recombinant MtSerRS | Methanothermobacter thermautotrophicus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Methanothermobacter thermautotrophicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine + tRNAArg | Methanothermobacter thermautotrophicus | - |
AMP + diphosphate + L-arginyl-tRNAArg | - |
? | |
| additional information | Methanothermobacter thermautotrophicus | arginyl-tRNA synthetase, MtArgRS, directly and stably interacts with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter thermautotrophicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GST-tagged MtArgRS from Escherichia coli strain BL21(DE3) by glutathione affinity chromatograophy. GST-MtArgRS shows the ability to co-purify with His-tagged MtSerRS by nickel affinity chromatography, co-elution of the two enzymes during gel filtration | Methanothermobacter thermautotrophicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine + tRNAArg | - |
Methanothermobacter thermautotrophicus | AMP + diphosphate + L-arginyl-tRNAArg | - |
? | |
| additional information | arginyl-tRNA synthetase, MtArgRS, directly and stably interacts with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C | Methanothermobacter thermautotrophicus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Arginyl-tRNA synthetase | - |
Methanothermobacter thermautotrophicus |
| ArgRS | - |
Methanothermobacter thermautotrophicus |
| MtArgRS | - |
Methanothermobacter thermautotrophicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Methanothermobacter thermautotrophicus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.026 | - |
tRNAArg | pH 7.5, 50°C, recombinant MtArgRS | Methanothermobacter thermautotrophicus | |
| 0.034 | - |
tRNAArg | pH 7.5, 50°C, recombinant MtArgRS in presence of recombinant MtSerRS | Methanothermobacter thermautotrophicus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Methanothermobacter thermautotrophicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Methanothermobacter thermautotrophicus | |
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