Any feedback?
Literature summary extracted from
- Proteolytic cleavage of the hyperthermophilic topoisomerase I from Thermotoga maritima does not impair its enzymatic properties (2004), Biochim. Biophys. Acta, 1700, 161-170.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.6.2.1 | - |
Thermotoga maritima |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 5.6.2.1 | topoisomerase I exhibits a unique hot spot susceptible to proteolytic attack with a variety of proteases (around amino acids 326-330). A truncated version of the enzyme lacking the C-terminal 93 amino acids is more susceptible to proteolysis, which suggests that the C-terminal region of the topoisomerase may be important to maintain the compact folding of the enzyme. Trypsin-digested topoisomerase I retains full DNA binding, cleavage and relaxation activities and full thermostability | Thermotoga maritima |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.6.2.1 | Thermotoga maritima | - |
- |
- |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
