Literature summary for 3.1.26.4 extracted from

Mukaiyama, A.; Takano, K.; Haruki, M.; Morikawa, M.; Kanaya, S.
Kinetically robust monomeric protein from a hyperthermophile (2004), Biochemistry, 43, 13859-13866 .

Search for more literature for 3.1.26.4

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	O74035	-	-
Thermococcus kodakarensis ATCC BAA-918	O74035	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
the denaturation by guanidinium chloride is completely reversible at 50°C, the unfolding and refolding reactions of the enzyme attain a two-state equilibrium in 2 weeks	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
Tk-Tk-RNase HII	-	Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
87.2	-	the denaturation temperature at a scan rate of 5°C/h is 87.2°C. The heat-induced unfolding of the enzyme does not attain equilibrium because of the slow unfolding	Thermococcus kodakarensis
89.2	-	the denaturation temperature at a scan rate of 90°C/h is 89.2°C. The heat-induced unfolding of the enzyme does not attain equilibrium because of the slow unfolding	Thermococcus kodakarensis

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Release 2023.1 (January 2023)