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Literature summary for 3.1.13.1 extracted from
- Comparison of EMSA and SPR for the characterization of RNA-RNase II complexes (2010), Protein J., 29, 394-397.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D201N | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D201N/E390A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D201N/Y313F | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D201N/Y313F/E390A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D207N | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D209N | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| D210N | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| E390A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| E542A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| F358A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| R500A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| Y253A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| Y253A/F358A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| Y313A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| Y313F | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
| Y313F/E390A | site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | complete inhibition | Escherichia coli |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNase II | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | stability of RNAse II-RNA interactions and effects on the enzyme reaction mechanism processing and degrading RNA molecules, analysis by surface plasmon resonance and electrophoretic mobility shift Assay, overview | Escherichia coli |
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