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Literature summary for 6.1.1.17 extracted from
- A chimeric glutamyl: glutaminyl-tRNA synthetase: implications for evolution (2008), Biochem. J., 15, 449-455.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the His-tagged chimeric mutant enzyme and of the catalytic domain of GluRS in Escherichia coli strain BL21(DE3) or the temperature sensitive strain JP1449(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a chimeric glutamyl:glutaminyl-tRNA synthetase, cGluGlnRS, consisting of the catalytic domain of the GluRS and the anti-codon binding domain of the GlnRS. In contrast to the isolated GluRS catalytic domain, the chimeric mutant shows detectable glutamylation activity with Escherichia coli tRNAGlu and is capable of complementing a ts-GluRS strain at non-permissive temperatures. The GlnRS anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation, interaction analysis, overview | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | Escherichia coli | wild-type enzyme and chimeric mutant cGluGlnRS, overview | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged chimeric mutant enzyme or catalytic domain of GluRS from strain BL21(DE3) or the temperature sensitive strain JP1449(DE3) by nickel affinity chromatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | wild-type enzyme and chimeric mutant cGluGlnRS, overview | Escherichia coli | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
| ATP + L-glutamate + tRNAGlu | analysis of domain functions in enzyme-substrate interactions, overview | Escherichia coli | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GluRS | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
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