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Literature summary for 3.1.11.5 extracted from
- Kinetics of ATP-stimulated nuclease activity of the Escherichia coli RecBCD enzyme (2006), J. Mol. Biol., 361, 954-968.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the nuclease reactions of the RecBCD-DNA complexes are initiated by mixing with ATP. The reaction is processive. The reaction begins near the 3'-end of the [5'-32P]DNA substrates and the major cleavage sites are two to four phosphodiester bonds apart. DNA cleavage is tightly coordinated with movement of the enzyme along the DNA. The reaction time-courses at low concentrations of ATP (0.1 mM and 0.025 mM) have a significant lag before cleavage products appear. We propose that the lag represents ATP-dependent movement of the DNA from an initial binding site in the helicase domain of the RecB subunit to the nuclease active site in a separate domain of RecB | Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| recBCD enzyme | - |
Escherichia coli |
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