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Literature summary for 4.6.1.24 extracted from
- Conformational stability of ribonuclease T1. II. Salt-induced renaturation (1979), J. Biochem., 86, 65-70.
General Stability
| General Stability | Organism |
|---|---|
| NaCl, protects from thermal denaturation, increases transition temperature, suppresses unfolding of enzyme by a denaturant, urea, increases conformational stability | Aspergillus oryzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| salts induce chain folding of disulfide-reduced and modified RNase T1 into native conformation, enzyme activity is not restored | Aspergillus oryzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| RNA + H2O | - |
Aspergillus oryzae | Hydrolyzed RNA | 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp | ? |  |
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