Any feedback?
Literature summary extracted from
- Conformational stability of ribonuclease T1. II. Salt-induced renaturation (1979), J. Biochem., 86, 65-70.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.6.1.24 | NaCl, protects from thermal denaturation, increases transition temperature, suppresses unfolding of enzyme by a denaturant, urea, increases conformational stability | Aspergillus oryzae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.24 | Aspergillus oryzae | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 4.6.1.24 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.24 | RNA + H2O | - |
Aspergillus oryzae | Hydrolyzed RNA | 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp | ? |  |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
