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Literature summary for 3.5.1.2 extracted from
- Molecular form and kinetic properties of phosphate-dependent glutaminase in the mitochondria isolated from the kidneys of normal and acidotic rats (1979), Biochim. Biophys. Acta, 567, 216-224.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| NH4+ | - |
Rattus norvegicus |  |
| phosphate | dependent on | Rattus norvegicus | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| glutamate | - |
Rattus norvegicus | |
| NaCl | - |
Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Rattus norvegicus | 5739 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gln + H2O | - |
Rattus norvegicus | Glu + NH3 | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
10 min, enzyme in whole kidney homogenate, phosphate-independent glutaminase is completly stable, phosphate-dependent glutaminase is completly denatured, preincubation with phosphate, phosphate-borate or bromothymol blue which induce aggregation of the enzyme molecules fully protects from heat inactivation | Rattus norvegicus |
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