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Literature summary for 3.1.26.4 extracted from
- HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors (2010), Viruses, 2, 900-926.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, overview | Escherichia coli |
| crystal structure analysis, overview | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | deletion of the basic loop in Escherichia coli RNase H inhibits but does not abolish activity. If the basic loop in Escherichia coli RNase H is inserted into an isolated inactive HIV-1 RNase H domain, Mn2+-dependent activity is partially restored | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | two Mg2+ ions in the RNase H active site, required. A two-metal ion mechanism requires that metal ion A activates a water molecule as a nucleophile and moves towards ion B, bringing the nucleophile in close proximity to the scissile bond, while metal ion B destabilizes the substrate-enzyme interaction and lowers the energy barrier to product formation | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids | ? | - |
? | |
| additional information | Homo sapiens | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids. A two-metal ion mechanism requires that metal ion A activates a water molecule as a nucleophile and moves towards ion B, bringing the nucleophile in close proximity to the scissile bond, while metal ion B destabilizes the substrate-enzyme interaction and lowers the energy barrier to product formation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids | Escherichia coli | ? | - |
? | |
| additional information | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids. A two-metal ion mechanism requires that metal ion A activates a water molecule as a nucleophile and moves towards ion B, bringing the nucleophile in close proximity to the scissile bond, while metal ion B destabilizes the substrate-enzyme interaction and lowers the energy barrier to product formation | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme shows a mixed beta-sheet with asymmetric alpha helices, and contains the C-helix, or basic loop, structure comparisons, overview | Escherichia coli |
| More | the enzyme shows a mixed beta-sheet with asymmetric alpha helices, and contains the C-helix, or basic loop, structure comparisons, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease H | - |
Escherichia coli |
| ribonuclease H | - |
Homo sapiens |
| RNase H | - |
Escherichia coli |
| RNase H | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | RNase H exists as a free enzyme | Escherichia coli |
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