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Literature summary for 3.1.26.4 extracted from
- Expression, purification, and crystallization of natural and selenomethionyl recombinant ribonuclease H from Escherichia coli (1990), J. Biol. Chem., 265, 13553-13559.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| natural and selenomethionyl recombinant enzyme | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
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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