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Literature summary for 5.6.2.1 extracted from
- Unmasking Anticooperative DNA-binding interactions of vaccinia DNA topoisomerase I (2007), Biochemistry, 46, 192-199.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vaccinia virus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP-independent breakage of single-stranded DNA, followed by passage and rejoining | Vaccinia DNA topoisomerase (vTopo) catalyzes highly specific nucleophilic substitution at a single phosphodiester linkage in the pentapyrimidine recognition sequence 5'-(C/T)+5C4+C3+T+2T+1pN-1 using an active-site tyrosine nucleophile, thereby expelling a 5'hydroxyl leaving group of the DNA. Equilibrium binding and cleavage measurements. Cleavage reactions and modified substrates for vTopo, kinetic and thermodynamic parameters for variable length vTopo substrates with guanine base substitutions and deletions are shown | Vaccinia virus |
aSynonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Vaccinia DNA topoisomerase I | - |
Vaccinia virus |
| vTopo | - |
Vaccinia virus |
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