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Literature summary for 3.1.26.4 extracted from
- Structural basis of the RNase H1 activity on stereo regular borano phosphonate DNA/RNA hybrids (2011), Biochemistry, 50, 3903-3912.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| analysis of the crystal structure of human RNase H1 in complex with a DNA/RNA duplex | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the DNA/RNA duplex SP hybrid is a substrate for the enzyme while the RP hybrid is not. Structure-activity relationship, and NMR analysis of structural features important for enzyme activity, overview. A fully RP BH3 DNA/RNA hybrid might not be a substrate for RNase H1, NMR structure. Structural analysis of stereoregular borano phosphate modifications | Homo sapiens | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNase H1 | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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