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Literature summary for 5.6.2.2 extracted from

  • Lamhasni, S.; Larsen, A.K.; Barray, M.; Monnot, M.; DeLain, E.; Fermandjian, S.
    Changes of self-association, secondary structure, and biological activity properties of topoisomerase II under varying salt conditions (1995), Biochemistry, 34, 3632-3639.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
network of DNA rings + ATP + H2O decatenation Saccharomyces cerevisiae monomeric DNA circles + ADP + phosphate
-
?
supercoiled DNA + ATP + H2O catenation Saccharomyces cerevisiae catenated DNA networks + ADP + phosphate
-
?
supercoiled DNA + ATP + H2O relaxation Saccharomyces cerevisiae relaxed DNA + ADP + phosphate
-
?

Subunits

Subunits Comment Organism
dimer 1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration Saccharomyces cerevisiae
monomer 1 * or 2 * 150000, the proportions of monomers and dimers in the monomer-dimer equilibrium strongly depends on both the protein concentration and the salt concentration Saccharomyces cerevisiae