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Literature summary for 5.6.2.2 extracted from

  • Vaughn, J.; Huang, S.; Wessel, I.; Sorensen, T.K.; Hsieh, T.; Jensen, L.H.; Jensen, P.B.; Sehested, M.; Nitiss, J.L.
    Stability of the topoisomerase II closed clamp conformation may influence DNA-stimulated ATP hydrolysis (2005), J. Biol. Chem., 280, 11920-11929.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DNA stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Homo sapiens
DNA stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzyme in yeast JELt1 cells Homo sapiens
overexpression of wild-type and mutant enzyme in yeast JELt1 cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
Y28F site-directed mutagenesis, mutation of an ATP hydrolysis domain residue of a bisdioxopiperazine- and sodium orthovanadate-resistant mutant enzyme, mutant shows reduced DNA-dependent ATP-hydrolysis activity without affecting the relaxation activity of the enzyme, no formation of the closed clamp conformation with vanadate or ADP, but with ADP-PNP Saccharomyces cerevisiae
Y50F site-directed mutagenesis, mutation of an ATP hydrolysis domain residue of a bisdioxopiperazine- and sodium orthovanadate-resistant mutant enzyme, mutant shows reduced DNA-dependent ATP-hydrolysis activity without affecting the relaxation activity of the enzyme, no formation of the closed clamp conformation with vanadate or ADP, but with ADP-PNP Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ADP traps the wild-type enzyme in the closed clamp formation, which shows no ATPase activity Homo sapiens
ADP traps the wild-type enzyme in the closed clamp formation, which shows no ATPAse hydrolysis activity Saccharomyces cerevisiae
bisdioxopiperazine inhibits the ATPase activity of the wild-type enzyme Homo sapiens
bisdioxopiperazine inhibits the ATPase activity of the wild-type enzyme Saccharomyces cerevisiae
sodium orthovanadate inhibits the ATPase activity of the wild-type enzyme, 50% inhibition at 0.005 mM, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y50F Homo sapiens
sodium orthovanadate noncompetitive, formation of a ternary enzyme-ADP-vanadate complex, inhibits the ATPase activity of the wild-type enzyme, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y28F Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information ATP hydrolysis kinetics for wild-type and Y28F mutant enzyme Saccharomyces cerevisiae
additional information
-
additional information ATP hydrolysis kinetics for wild-type and Y50F mutant enzyme Homo sapiens
0.2
-
ATP pH 7.7, 30°C, recombinant Y28F mutant enzyme Saccharomyces cerevisiae
0.3
-
ATP pH 7.7, 30°C, recombinant wild-type enzyme Saccharomyces cerevisiae
0.3
-
ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme Homo sapiens
0.5
-
ATP pH 7.7, 30°C, recombinant wild-type enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Homo sapiens 5634
-
nucleus
-
Saccharomyces cerevisiae 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
KCl
-
Homo sapiens
KCl
-
Saccharomyces cerevisiae
Mg2+
-
Homo sapiens
Mg2+
-
Saccharomyces cerevisiae
NaCl
-
Homo sapiens
NaCl
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isozyme IIalpha
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + ATP cleavage requires coupling to ATP hydrolysis Homo sapiens ?
-
?
DNA + ATP + H2O relaxation and cleavage of DNA, cleavage requires coupling to ATP hydrolysis Saccharomyces cerevisiae DNA + ADP + phosphate
-
?
additional information the enzyme performs ATP hydrolysis activity Homo sapiens ?
-
?
additional information the enzyme performs ATP hydrolysis activity Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
More stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Homo sapiens
More stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Top2
-
Homo sapiens
Top2
-
Saccharomyces cerevisiae
Top2alpha
-
Homo sapiens
Topoisomerase II
-
Homo sapiens
Topoisomerase II
-
Saccharomyces cerevisiae
topoisomerase IIalpha
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens
30
-
assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.5
-
ATP pH 7.7, 30°C, recombinant wild-type or Y50F mutant enzyme, in absence of DNA Homo sapiens
1
-
ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in absence of DNA Saccharomyces cerevisiae
1.1
-
ATP pH 7.7, 30°C, recombinant wild-type enzyme, in absence of DNA Saccharomyces cerevisiae
1.2
-
ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA Saccharomyces cerevisiae
1.5
-
ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA Homo sapiens
3.6
-
ATP pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA Homo sapiens
3.6
-
ATP pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
assay at, ATP hydrolysis assay Homo sapiens
8
-
assay at, DNA relaxation assay Homo sapiens
8
-
assay at, DNA relaxation assay Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Homo sapiens
ATP stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis Saccharomyces cerevisiae