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Literature summary for 3.1.26.4 extracted from

  • You, D.J.; Chon, H.; Koga, Y.; Takano, K.; Kanaya, S.
    Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring (2007), Biochemistry, 46, 11494-11503.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure is determined at 1.6 A resolution, crystals are grown by the sitting-drop vapor-diffusion method at 4°C Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
R118A the specific activities of R118A-RNase HI for both 12-bp RNA/DNA and RNA/RNA substrates are reduced by approximately 10fold as compared to those of the wild-type protein Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii F9VN79
-
-
Sulfurisphaera tokodaii 7 F9VN79
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNA/DNA hybrid + H2O
-
Sulfurisphaera tokodaii ?
-
?
RNA/DNA hybrid + H2O
-
Sulfurisphaera tokodaii 7 ?
-
?

Synonyms

Synonyms Comment Organism
ribonuclease HI
-
Sulfurisphaera tokodaii
Sto-RNase HI
-
Sulfurisphaera tokodaii
type 1 ribonuclease H
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
78
-
Tm-value for mutant enzyme DELTAC6 Sulfurisphaera tokodaii
93
-
Tm-value for mutant enzyme C58/145A Sulfurisphaera tokodaii
102
-
Tm-value for wild-type enzyme. The thermostable protein is destabilized by elimination of the disulfide bond and C-terminal truncation Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Sulfurisphaera tokodaii