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Literature summary for 3.1.26.4 extracted from
- The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H (2008), J. Mol. Biol., 384, 531-539.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | populating the folded region of the intermediate mimic by protein engineering | Thermus thermophilus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 12800 | - |
intermediate mimic, ultracentrifugation experiments | Thermus thermophilus |
| 13000 | - |
intermediate mimic, gel filtration | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | P29253 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA agarose and reverse-phase HPLC | Thermus thermophilus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | enzyme is composed of five alpha-helices (A to E) and five beta-strands (I to V). The intermediate mimic is a monomer | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease H | - |
Thermus thermophilus |
| RNase H | - |
Thermus thermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
melting temperature curve of the intermediate mimic shown. The heat denaturation experiment shows that this intermediate mimic unfolds cooperatively as temperature increases, with a melting temperature (Tm) of about 75°C | Thermus thermophilus |
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Release 2023.1 (January 2023)
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