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Literature summary for 3.1.21.5 extracted from
- Mutual activation of two restriction endonucleases: interaction of EcoP1 and EcoP15 (1998), Biol. Chem., 379, 617-620.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
EcoP15 | - |
| Escherichia coli | - |
EcoPI | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DNA + H2O | recognizes nonsymetric nucleotide sequences. A necessary condition for DNA cleavage is the presence of two unmethylated recognition sites which are inversely, head-to-head, oriented in the DNA double strand. A DNA substrate possessing one EcoP1 and one EcoP15 site in the head to head configuration can not be cleaved by an individual enzyme, however it is specifically digested in the simultaneously presence of both enzymes. The two different type III enzymes can functionally cooperate in the cleavage of DNA | Escherichia coli | specific double-stranded DNA fragments with terminal 5'-phosphate | - |
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