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Literature summary for 3.1.26.4 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

General Stability Organism
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

Organism UniProt Comment Textmining
Thermococcus kodakarensis
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-
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Synonyms

Synonyms Comment Organism
RNase H2
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Thermococcus kodakarensis