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Literature summary extracted from

  • Okada, J.; Koga, Y.; Takano, K.; Kanaya, S.
    Slow unfolding pathway of hyperthermophilic Tk-RNase H2 examined by pulse proteolysis using the stable protease Tk-subtilisin (2012), Biochemistry, 51, 9178-9191.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.1.26.4 ribonuclease H2 from Thermococcus kodakarensis is stabilized by its remarkably slow unfolding rate in guanidine hydrochloride, making the native state of RNase H2 completely resistant to subtilisin Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Thermococcus kodakarensis
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3.4.21.B57 Thermococcus kodakarensis P58502
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.B57 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 ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.26.4 RNase H2
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 Thermococcus kodakarensis
3.4.21.B57 Tk-subtilisin
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 Thermococcus kodakarensis