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Literature summary for 3.1.21.5 extracted from
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes (2007), EMBO J., 26, 3815-3825.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| study of enzyme-DNA pre-cleavage complexes by atomic force microscopy. DNA loops observed are formed by a contact between site-bound EcoP15I enzyme and a nonspecific region of DNA, and do not result from translocation. Model for restricition by type III enzymes involving both structural elements, and a functional reason for the unusual site orientation required for the cleavage reaction | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
P15I | - |
| Escherichia coli P15I | - |
P15I | - |
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Release 2023.1 (January 2023)
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