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Literature summary for 3.1.26.3 extracted from
- Base substitutions at scissile bond sites are sufficient to alter RNA-binding and cleavage activity of RNase III (2011), FEMS Microbiol. Lett., 315, 30-37.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | substrate is bdm mRNA with recombinant His-tagged RNase III. Introduction of random mutations at the RNase III cleavages sites in bdm mRNA alter the enzyme activity, secondary structures and the stability of hairpins containing the RNase III cleavage sites 3 and 4-II, and RNase II cleavage patterns, overview | Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNase III | - |
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 |
|---|---|---|---|
| 7.9 | - |
assay at | Escherichia coli |
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Release 2023.1 (January 2023)
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