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Literature summary for 3.4.21.B57 extracted from
- Slow unfolding pathway of hyperthermophilic Tk-RNase H2 examined by pulse proteolysis using the stable protease Tk-subtilisin (2012), Biochemistry, 51, 9178-9191.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | P58502 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Tk-RNase H2 + H2O | ribonuclease H2 from Thermococcus kodakarensis, pulse proteolysis using the superstable subtilisin-like serine protease Tk-subtilisin in highly concentrated guanidine hydrochloride to unfold the highly stable substrate protein. The native state of Tk-RNase H2 is completely resistant to Tk-subtilisin, whereas the unfolded state (induced by 4 M GdnHCl) is degraded by Tk-subtilisin, identification of the cleavage sites. Structure analysis of unfolded substrate states | Thermococcus kodakarensis | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tk-subtilisin | - |
Thermococcus kodakarensis |
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Release 2023.1 (January 2023)
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