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Literature summary for 3.1.26.4 extracted from
- Sequence-specific cleavage of RNA by hybrid ribonuclease H (1994), FEBS Lett., 339, 67-72.
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | hybrid RNase H molecules with various oligodeoxyribonucleotides may facilitate structural studies of RNA and prove useful as tool for RNA manipulations | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a Cys residue is substituted for Glu135 by site-directed mutagenesis in the mutant enzyme, in which all 3 free Cys residues are replaced by Ala and coupled with a maleimide group which is attached to the 5'-terminus of the nonadeoxyribonucleotide, 5'-GTCATCTCC-3', with a flexible tether. The resulting hybrid enzyme d9-C135/RNase H shows site-specific cleavage of the 22-base RNA, 132-base RNA and 534-base RNA which contain a single target sequence, primarily at the unique phosphodiester bond within the target sequence. The hybrid enzyme performs multiple turnovers and at a substrate/enzyme ratio of 10:1 the RNAs are almost completely cleaved | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| RNA-DNA hybrid + H2O | - |
Escherichia coli | ribonucleotide 5'-phosphomonoester | - |
? |  |
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