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Literature summary for 5.6.2.2 extracted from

  • Mueller-Planitz, F.; Herschlag, D.
    Interdomain communication in DNA topoisomerase II. DNA binding and enzyme activation (2006), J. Biol. Chem., 281, 23395-23404.
    View publication on PubMed
Search for more literature for 5.6.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of full-length Saccharomyces cerevisiae topoisomerase II fused to an intein and a chitin binding domain affinity tag in the yeast strain BCY123 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
Y782F mutation within the G-DNA binding site. Mutation affects DNA cleavage but has negligible effects on steady state ATP hydrolysis Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information G-DNA binds with higher affinity than T-DNA. enzyme with only G-DNA bound is competent to cleave DNA and the ATPase activity of enzyme solely bound to G-DNA is partially stimulated. Full stimulation requires binding of T-DNA Saccharomyces cerevisiae ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.23
-
 ATP wild-type, pH 7.5 Saccharomyces cerevisiae
0.28
-
 ATP mutant Y782F, pH 7.5 Saccharomyces cerevisiae
5.6
-
 ATP mutant Y782F, presence of 68 bp DNA duplex, pH 7.5 Saccharomyces cerevisiae
7.2
-
 ATP wild-type, presence of 68 bp DNA duplex, pH 7.5 Saccharomyces cerevisiae