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Literature summary for 6.3.1.2 extracted from
- Urea-induced dissociation and unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric and spectral studies (1995), Protein Sci., 4, 1544-1552.
General Stability
| General Stability | Organism |
|---|---|
| below 2 M urea the enzyme retains its dodecameric structure and full catalytic activity. In 6 M urea, dissociation into subunits | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51800 | - |
x * 51800, sedimentation equilibrium experiments in 6 M urea | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-Glu + NH4+ | - |
Escherichia coli | ADP + phosphate + L-Gln | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 51800, sedimentation equilibrium experiments in 6 M urea | Escherichia coli |
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