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Literature summary for 5.6.2.1 extracted from
- Revealing the mode of action of DNA topoisomerase I and its inhibitors by atomic force microscopy (2003), Biochem. Biophys. Res. Commun., 301, 789-797.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| camptothecin | in presence of the inhibitor, enzyme-supercoiled DNA complexes in which the enzyme is locked inside a relaxed region of the supercoiled DNA molecule are observed | Bos taurus |  |
| tyrophostin AG-1387 | the inhibitor alters the DNA relaxation process producing unique shapes of DNA molecules | Bos taurus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| supercoiled DNA | the enzyme relaxes supercoiled DNA starting from a certain point in the DNA molecules and proceeds in one direction towards one of the edges of the DNA molecule. The relaxation of the supercoiled DNA is subsequently followed by a knotting event | Bos taurus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| topo IB | - |
Bos taurus |
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Release 2023.1 (January 2023)
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