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Literature summary extracted from
- Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues (2010), Biochemistry, 49, 5167-5175.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | expression of recombinant chimeric and point mutant enzymes in Escherichia coli strain BL21(DE3), I53 and L56 point mutants are expressed insolubly in inclusion bodies | Chlorobaculum tepidum |
| 3.1.26.4 | expression of recombinant chimeric mutant enzyme and of His-tagged mutant L56S in Escherichia coli strain BL21(DE3) | Thermus thermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | I53A | site-directed mutagenesis | Chlorobaculum tepidum |
| 3.1.26.4 | I53D | site-directed mutagenesis | Chlorobaculum tepidum |
| 3.1.26.4 | L56A | site-directed mutagenesis | Chlorobaculum tepidum |
| 3.1.26.4 | L56D | site-directed mutagenesis | Chlorobaculum tepidum |
| 3.1.26.4 | L56S | site-directed mutagenesis | Thermus thermophilus |
| 3.1.26.4 | L56S | site-directed mutagenesis | Chlorobaculum tepidum |
| 3.1.26.4 | additional information | construction of chimeric proteins of the Thermus thermophilus enzyme with the folding core of Chlorobium tepidum RNaseH, thermal stability analysis, overview | Thermus thermophilus |
| 3.1.26.4 | additional information | construction of chimeric proteins of the Thermus thermophilus enzyme with the folding core of Chlorobium tepidum RNaseH, thermal stability analysis, overview | Chlorobaculum tepidum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.26.4 | additional information | - |
additional information | thermodynamic analyses of chimeric proteins, overview | Chlorobaculum tepidum | |
| 3.1.26.4 | additional information | - |
additional information | thermodynamic analyses of mutant enzymes, overview | Thermus thermophilus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.4 | Chlorobaculum tepidum | - |
- |
- |
| 3.1.26.4 | Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | recombinant recombinant chimeric and point mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography | Chlorobaculum tepidum |
| 3.1.26.4 | recombinant recombinant chimeric mutant enzyme from Escherichia coli strain BL21(DE3) by heparin affinity chromatography, and His-tagged mutant L56S by nickel affinitychromatography | Thermus thermophilus |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | recombinant I53 and L56 point mutants after being expressed insolubly in inclusion bodies in Escherichia coli | Chlorobaculum tepidum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | CtepRNH | - |
Chlorobaculum tepidum |
| 3.1.26.4 | RNase H | - |
Thermus thermophilus |
| 3.1.26.4 | RNase H | - |
Chlorobaculum tepidum |
| 3.1.26.4 | TthRNH | - |
Thermus thermophilus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | additional information | - |
analysis of thermal unfolding, the folding core of Chlorobium tepidum RNaseH plays an important role in the unfolded state of this protein | Chlorobaculum tepidum |
| 3.1.26.4 | additional information | - |
analysis of thermal unfolding, the folding core of Thermus thermophilus RNaseH plays an important role in the unfolded state of this protein | Thermus thermophilus |
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