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Literature summary extracted from
- The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution (2001), Eur. J. Biochem., 268, 3993-4000.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.6.1.24 | two crystal forms obtained, the classic crystal form I, and the crystals of form II, obtained by repeated seeding | Aspergillus oryzae |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.6.1.24 | the enzyme is remarkably stable at high salt concentrations | Aspergillus oryzae |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.24 | Ca2+ | the enzyme has six binding sites for the cation | Aspergillus oryzae |  |
| 4.6.1.24 | Sr2+ | the enzyme contains a divalent ion-binding site involving Asp49, with preference for this cation. The ion binding at this site stabilizes the protein | Aspergillus oryzae | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.24 | Aspergillus oryzae | - |
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Release 2023.1 (January 2023)
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