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Literature summary for 3.1.21.10 extracted from
- The interaction of four-way DNA junctions with resolving enzymes (2010), Biochem. Soc. Trans., 38, 399-403.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| resolving enzymes bound to DNA junctions, X-ray diffraction structure determination and analysis | Homo sapiens |
| resolving the enzyme bound to DNA junctions, X-ray diffraction structure determination and analysis | Escherichia phage T7 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | strong inhibition | Escherichia phage T7 |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | cleavage of a four-way DNA junction by the human SLX1-SLX4 complex, overview | ? | - |
? | |
| additional information | Escherichia phage T7 | endonuclease I catalyses the breakage of the P-O3' bond | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia phage T7 | - |
- |
- |
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HEK-293 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | cleavage of a four-way DNA junction by the human SLX1-SLX4 complex, overview | Homo sapiens | ? | - |
? | |
| additional information | endonuclease I catalyses the breakage of the P-O3' bond | Escherichia phage T7 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | the endonuclease I forms an intimately associated symmetrical homodimer comprising two domains, each formed by residues 17-44 from one subunit and 50-145 from the other. The domains are connected by a bridge that forms part of an extended beta-sheet | Escherichia phage T7 |
| More | model of DNA bound in the active site of phage T7 endonuclease I | Escherichia phage T7 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | the enzyme belongs to the nuclease superfamily, and is clearly related to the restriction enzymes | Escherichia phage T7 |
| phage T7 endonuclease I | - |
Homo sapiens |
| phage T7 endonuclease I | - |
Escherichia phage T7 |
| phage T7 junction-resolving enzyme endonuclease I | - |
Homo sapiens |
| phage T7 junction-resolving enzyme endonuclease I | - |
Escherichia phage T7 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | recognition and manipulation of junction structure, overview | Homo sapiens |
| additional information | recognition and manipulation of junction structure, overview. Model of DNA bound in the active site of phage T7 endonuclease I | Escherichia phage T7 |
| physiological function | four-way DNA Holliday junctions are resolved into duplex species by the action of the junction-resolving enzymes, nucleases selective for the structure of helical branchpoints. Mechanism of structural selectivity of these enzymes, overview | Homo sapiens |
| physiological function | four-way DNA Holliday junctions are resolved into duplex species by the action of the junction-resolving enzymes, nucleases selective for the structure of helical branchpoints. Mechanism of structural selectivity of these enzymes, overview | Escherichia phage T7 |
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Release 2023.1 (January 2023)
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