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Literature summary for 6.1.1.16 extracted from
- Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase (2006), Biochemistry, 45, 6835-6845.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged wild-type enzyme and halophilic-specific peptide mutant enzyme variants in Escherichia coli strain BL21(DE3) | Halobacterium sp. |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D239A/D240A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Halobacterium sp. |
| D417A/E420A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Halobacterium sp. |
| D435A/D436A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Halobacterium sp. |
| additional information | deletion of the halophilic-specific peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, maintaining the peptide length but substituting acidic residues in the peptide with neutral or basic residues has no major deleterious effect, suggesting that the acidity of the peptide is not important for the kcat of tRNA aminoacylation, construction of point mutants and deletion mutants, e.g. deletion mutant DELTA193-212, overview | Halobacterium sp. |
General Stability
| General Stability | Organism |
|---|---|
| instability of the enzyme without the halophilic-specific peptide | Halobacterium sp. |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5'-O-[N-(L-cysteinyl)sulfamoyl] adenosine | i.e. Cys-AMS, a cysteinyl adenylate analogue | Halobacterium sp. |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0012 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D417A/E420A | Halobacterium sp. | |
| 0.0013 | - |
tRNACys | pH 7.5, 40°C, recombinant wild-type enzyme | Halobacterium sp. | |
| 0.0017 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D239A/D240A | Halobacterium sp. | |
| 0.0023 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D435A/D436A | Halobacterium sp. | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Halobacterium sp. | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-cysteine + tRNACys | Halobacterium sp. | - |
AMP + diphosphate + L-cysteinyl-tRNACys | - |
? | |
| ATP + L-cysteine + tRNACys | Halobacterium sp. NRC-1 | - |
AMP + diphosphate + L-cysteinyl-tRNACys | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Halobacterium sp. | - |
- |
- |
| Halobacterium sp. NRC-1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type enzyme and halophilic-specific peptide mutant enzyme variants from Escherichia coli strain BL21(DE3) | Halobacterium sp. |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Halobacterium sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-cysteine + tRNACys | - |
Halobacterium sp. | AMP + diphosphate + L-cysteinyl-tRNACys | - |
? | |
| ATP + L-cysteine + tRNACys | - |
Halobacterium sp. NRC-1 | AMP + diphosphate + L-cysteinyl-tRNACys | - |
? | |
| additional information | Halobacterium sp. contains an unusual peptide that is unique to several halophile archaeal CysRS, which catalyze attachment of cysteine to tRNACys to generate the essential cysteinyl-tRNACys required for protein synthesis, deletion of the peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, the acidity of the peptide is not important for the kcat of tRNA aminoacylation | Halobacterium sp. | ? | - |
? | |
| additional information | Halobacterium sp. contains an unusual peptide that is unique to several halophile archaeal CysRS, which catalyze attachment of cysteine to tRNACys to generate the essential cysteinyl-tRNACys required for protein synthesis, deletion of the peptide reduces the catalytic efficiency of aminoacylation by a factor of 100 that largely results from a defect in kcat, rather than the Km for tRNACys, the acidity of the peptide is not important for the kcat of tRNA aminoacylation | Halobacterium sp. NRC-1 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CysRS | - |
Halobacterium sp. |
| Cysteinyl-tRNA synthetase | - |
Halobacterium sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Halobacterium sp. |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.014 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D417A/E420A | Halobacterium sp. | |
| 0.03 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D435A/D436A | Halobacterium sp. | |
| 0.06 | - |
tRNACys | pH 7.5, 40°C, recombinant mutant D239A/D240A | Halobacterium sp. | |
| 0.11 | - |
tRNACys | pH 7.5, 40°C, recombinant wild-type enzyme | Halobacterium sp. | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Halobacterium sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Halobacterium sp. | |
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