Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.2 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
5.6.2.2 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

EC Number Inhibitors Comment Organism Structure
5.6.2.2 ADP traps the wild-type enzyme in the closed clamp formation, which shows no ATPase activity Homo sapiens
5.6.2.2 ADP traps the wild-type enzyme in the closed clamp formation, which shows no ATPAse hydrolysis activity Saccharomyces cerevisiae
5.6.2.2 bisdioxopiperazine inhibits the ATPase activity of the wild-type enzyme Homo sapiens
5.6.2.2 bisdioxopiperazine inhibits the ATPase activity of the wild-type enzyme Saccharomyces cerevisiae
5.6.2.2 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
5.6.2.2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.2.2 additional information
-
 additional information ATP hydrolysis kinetics for wild-type and Y28F mutant enzyme Saccharomyces cerevisiae
5.6.2.2 additional information
-
 additional information ATP hydrolysis kinetics for wild-type and Y50F mutant enzyme Homo sapiens
5.6.2.2 0.2
-
 ATP pH 7.7, 30°C, recombinant Y28F mutant enzyme Saccharomyces cerevisiae
5.6.2.2 0.3
-
 ATP pH 7.7, 30°C, recombinant wild-type enzyme Saccharomyces cerevisiae
5.6.2.2 0.3
-
 ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme Homo sapiens
5.6.2.2 0.5
-
 ATP pH 7.7, 30°C, recombinant wild-type enzyme Homo sapiens

Localization

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.2 Homo sapiens
-
 isozyme IIalpha
-
5.6.2.2 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.2.2 30
-
 assay at Homo sapiens
5.6.2.2 30
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.2.2 0.5
-
 ATP pH 7.7, 30°C, recombinant wild-type or Y50F mutant enzyme, in absence of DNA Homo sapiens
5.6.2.2 1
-
 ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in absence of DNA Saccharomyces cerevisiae
5.6.2.2 1.1
-
 ATP pH 7.7, 30°C, recombinant wild-type enzyme, in absence of DNA Saccharomyces cerevisiae
5.6.2.2 1.2
-
 ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA Saccharomyces cerevisiae
5.6.2.2 1.5
-
 ATP pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA Homo sapiens
5.6.2.2 3.6
-
 ATP pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA Homo sapiens
5.6.2.2 3.6
-
 ATP pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6.2.2 7.7
-
 assay at, ATP hydrolysis assay Homo sapiens
5.6.2.2 8
-
 assay at, DNA relaxation assay Homo sapiens
5.6.2.2 8
-
 assay at, DNA relaxation assay Saccharomyces cerevisiae

Cofactor

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