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Literature summary for 4.6.1.24 extracted from
- Probing the effect of water-water interactions on enzyme activity with salt gradients: a case-study using ribonuclease t1 (2010), J. Phys. Chem. B, 114, 16918-16928.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Aspergillus oryzae | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GpC + H2O | enzyme-catalyzed hydrolysis of GpC | Aspergillus oryzae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNase T1 | - |
Aspergillus oryzae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
assay at | Aspergillus oryzae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | effects of water-water hydrogen bonding types upon the activity of the enzyme ribonuclease t1 through perturbation of the water hydrogen bonding distribution by using various salts, overview. Various salts differ in their ability to reduce the enzymatic activity of ribonuclease t1 correlated with the ability of each salt to promote high-angle hydrogen bonding in water. Increasing the population of high-angle hydrogen bonds among water molecules stabilizes the more compact, less active conformations of the enzyme | Aspergillus oryzae |
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Release 2023.1 (January 2023)
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