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Literature summary for 6.1.1.19 extracted from
- Expression and properties of arginyl-tRNA synthetase from jack bean (Canavalia ensiformis) (2008), Protein Expr. Purif., 61, 163-167.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene argS, DNA and amino acid sequence determination and analysis, expression of N-terminally HIS-/thioredoxin-tagged enzyme in Escherichia coli strain BL21 | Canavalia ensiformis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | 50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme | Canavalia ensiformis |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00086 | - |
tRNAArg ACG | pH 7.5, 30°C, recombinant detagged enzyme | Canavalia ensiformis | |
| 0.00184 | - |
tRNAArg ACG | pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme | Canavalia ensiformis | |
| 0.0164 | - |
L-arginine | pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme | Canavalia ensiformis | |
| 0.0196 | - |
L-arginine | pH 7.5, 30°C, recombinant detagged enzyme | Canavalia ensiformis | |
| 0.186 | - |
ATP | pH 7.5, 30°C, recombinant detagged enzyme | Canavalia ensiformis | |
| 0.207 | - |
ATP | pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme | Canavalia ensiformis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Canavalia ensiformis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine + tRNAArg | Canavalia ensiformis | - |
AMP + diphosphate + L-arginyl tRNAArg | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Canavalia ensiformis | B2G3G6 | gene argS | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| soluble recombinant N-terminally HIS-/thioredoxin-tagged enzyme from Escherichia coli strain BL21 by metal affinity chromatography, tag cleavage by thrombin | Canavalia ensiformis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | enzyme expression | Canavalia ensiformis | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activity of recombinant tagged and detagged enzyme | Canavalia ensiformis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine + tRNAArg | - |
Canavalia ensiformis | AMP + diphosphate + L-arginyl tRNAArg | - |
? | |
| ATP + L-arginine + tRNAArg ACG | tRNA substrate from Escherichia coli | Canavalia ensiformis | AMP + diphosphate + L-arginyl tRNAArg ACG | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Arginyl-tRNA synthetase | - |
Canavalia ensiformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Canavalia ensiformis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.215 | - |
L-arginine | pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme | Canavalia ensiformis | |
| 0.337 | - |
L-arginine | pH 7.5, 30°C, recombinant detagged enzyme | Canavalia ensiformis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.2 | - |
about | Canavalia ensiformis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9.5 | activity range, pH-profile, overview | Canavalia ensiformis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Canavalia ensiformis | |
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