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Literature summary for 3.1.26.4 extracted from
- Characterization of a new RNase HII and its essential amino acid residues in the archaeon Sulfolobus tokodaii reveals a regulatory C-terminus (2010), Biochemistry (Moscow), 75, 930-937.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D7N | site-directed mutagenesis | Sulfurisphaera tokodaii |
| E8Q | site-directed mutagenesis | Sulfurisphaera tokodaii |
| additional information | truncated mutant ST0519_1-195 retains only partial activity, while truncated mutant ST0519_1-196 completely loses its activity. Computational analysis of the substrate binding site through construction of diverse truncation mutants, overview | Sulfurisphaera tokodaii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | - |
Sulfurisphaera tokodaii |  |
| Co2+ | - |
Sulfurisphaera tokodaii | |
| Mn2+ | the activity of wild-type protein is stimulated by Mn2+, whereas this cation significantly inhibits the activity of C-terminal truncated mutant proteins | Sulfurisphaera tokodaii | |
| Ni2+ | - |
Sulfurisphaera tokodaii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates | Sulfurisphaera tokodaii | |
| Mn2+ | the activity of wild-type protein is stimulated by Mn2+, whereas this cation significantly inhibits the activity of C-terminal truncated mutant proteins | Sulfurisphaera tokodaii | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfurisphaera tokodaii | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme utilizes hybrid RNA/DNA as a substrate. Cleavage activity of RNase HII with different oligomeric substrates, overview | Sulfurisphaera tokodaii | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the RNase HII contains a regulatory C-terminal tail. The C-terminus might form a short alpha-helix in which two residues, I195 and L196, are essential for the cleavage activity. The C-terminal alpha-helix is likely involved in the Mn2+-dependent substrate cleavage activity through stabilization of a flexible loop structure | Sulfurisphaera tokodaii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNase HII | - |
Sulfurisphaera tokodaii |
| ST0519 | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 50 | - |
Sulfurisphaera tokodaii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 70 | activity profile | Sulfurisphaera tokodaii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Sulfurisphaera tokodaii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the RNase HII contains a regulatory C-terminal tail. The C-terminus might form a short alpha-helix in which two residues, I195 and L196, are essential for the cleavage activity. The C-terminal alpha-helix is likely involved in the Mn2+-dependent substrate cleavage activity through stabilization of a flexible loop structure. Structure and function of both archaeal RNase HII, overview | Sulfurisphaera tokodaii |
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