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Literature summary for 6.3.1.2 extracted from
- Regulation of ammonium assimilation in Haloferax mediterranei: interaction between glutamine synthetase and two GlnK proteins (2013), Biochim. Biophys. Acta, 1834, 16-23.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-oxoglutarate | activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein | Haloferax mediterranei |  |
| GlnK1 protein | activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein | Haloferax mediterranei | |
| GlnK2 protein | activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein | Haloferax mediterranei | |
| protein GlnK1 | GlnK1 and GlnK2 activate glutamine synthetase in vitro in the presence of 2-oxoglutarate. Enzyme activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18fold in the presence of both 2-oxoglutarate and one GlnK | Haloferax mediterranei | |
| protein GlnK2 | GlnK1 and GlnK2 activate glutamine synthetase in vitro in the presence of 2-oxoglutarate. Enzyme activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18fold in the presence of both 2-oxoglutarate and one GlnK | Haloferax mediterranei |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene glnA, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLys in inclusion bodies | Haloferax mediterranei |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| AMP | 1 mM, 50% inhibition | Haloferax mediterranei | |
| glutamine | 2.5 mM, 50% inhibition | Haloferax mediterranei | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Haloferax mediterranei | |
| Mg2+ | the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+ | Haloferax mediterranei | |
| Mn2+ | the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+ | Haloferax mediterranei | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50500 | - |
12 * 50500, about, sequence calculation | Haloferax mediterranei |
| 580000 | - |
recombinant enzyme, gel filtration | Haloferax mediterranei |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | Haloferax mediterranei | - |
ADP + phosphate + L-glutamine | - |
? | |
| additional information | Haloferax mediterranei | regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax mediterranei | B8ZJH0 | gene glnA | - |
| Haloferax mediterranei | F2RM17 | - |
- |
| Haloferax mediterranei DSM 3757 | F2RM17 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Haloferax mediterranei |
| refolded recombinant nearly pure enzyme by anion exchange chromatography | Haloferax mediterranei |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| recombinant His-tagged nearly pure glutamine synthetase from inclusion bodies is solubilised at 37°C using 8 M urea as chaotrope in 20 mM Tris-HCl, pH 8.0, containing 2 mM EDTA and 50 mM DTT. The solubilised protein is then diluted in 20 mM Tris-HCl, pH 7.5, with 2 M NaCl and 5 mM DTT to a final protein concentration of 0.02 mg/ml and kept overnight at room temperature to enable proper folding | Haloferax mediterranei |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, 2 M NaCl, 1 week, stable | Haloferax mediterranei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | - |
Haloferax mediterranei | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | - |
Haloferax mediterranei DSM 3757 | ADP + phosphate + L-glutamine | - |
? | |
| additional information | regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate | Haloferax mediterranei | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dodecamer | - |
Haloferax mediterranei |
| dodecamer | 12 * 50500, about, sequence calculation | Haloferax mediterranei |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlnA | - |
Haloferax mediterranei |
| Glutamine synthetase | - |
Haloferax mediterranei |
| GS3 | - |
Haloferax mediterranei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42 | - |
assay at | Haloferax mediterranei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Haloferax mediterranei |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Haloferax mediterranei | |
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