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Literature summary extracted from
- Hyperthermophilic topoisomerase I from Thermotoga maritima A very efficient enzyme that functions independently of zinc binding (2001), J. Biol. Chem., 276, 46495-46503 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.6.2.1 | overexpressed in Escherichia coli | Thermotoga maritima |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.6.2.1 | C559A/C561A | no detectable zinc is bound to the mutant enzyme and its fluorescence properties are modified, suggesting a change of conformation in the protein lacking zinc. GThe mutant enzyme exhibits an activity similar to that of the wild-type enzyme with the same optimal temperature for activity. Thermostability is not affected by the mutation. Decatenase activity of wild type and C559A/C561A mutant enzymes shows no significant difference. Cleavage positions obtained with the C559A/C561A mutant is similar to those observed with the wild type enzyme. Preference for cytosine at position -4 is retained, and cleavage intensities are comparable | Thermotoga maritima |
| 5.6.2.1 | Y288F | totally inactive protein | Thermotoga maritima |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.6.2.1 | additional information | zinc binding is not required for DNA relaxation activity | Thermotoga maritima |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.6.2.1 | Thermotoga maritima | P46799 | - |
- |
| 5.6.2.1 | Thermotoga maritima DSM 3109 | P46799 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.6.2.1 | wild-type enzyme and mutant enzymes Y288F and C559A/C561A | Thermotoga maritima |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.6.2.1 | DNA | the enzyme exhibits a very high DNA relaxing activity. Strong preference for a cytosine at position -4 of the cleavage | Thermotoga maritima | ? | - |
? |  |
| 5.6.2.1 | DNA | the enzyme exhibits a very high DNA relaxing activity. Strong preference for a cytosine at position -4 of the cleavage | Thermotoga maritima DSM 3109 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.6.2.1 | ? | x * 76000, SDS-PAGE | Thermotoga maritima |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.6.2.1 | Topoisomerase I | - |
Thermotoga maritima |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.1 | 50 | - |
assay at | Thermotoga maritima |
| 5.6.2.1 | 70 | 75 | - |
Thermotoga maritima |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.1 | 80 | - |
both wild type and C559A/C561A mutant enzymes remain fully active after 30 min | Thermotoga maritima |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.1 | 8 | - |
assay at | Thermotoga maritima |
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Release 2023.1 (January 2023)
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