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Literature summary extracted from

  • Sorensen, T.K.; Grauslund, M.; Jensen, P.B.; Sehested, M.; Jensen, L.H.
    Separation of bisdioxopiperazine- and vanadate resistance in topoisomerase II (2005), Biochem. Biophys. Res. Commun., 334, 853-860.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.6.2.2 vanadate slight activation of mutant L169F Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.2.2 overexpression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain JelDELTATop1 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.2 L169F site-directed mutagenesis, the mutant enzyme is highly resistant to vanadate, the mutant shows reduced DNA passage activity compared to the wild-type enzyme Homo sapiens
5.6.2.2 L169I site-directed mutagenesis, the mutant shows unaltered DNA passage activity and slightly reduced DNA hyperstimulation compared to the wild-type enzyme Homo sapiens
5.6.2.2 R162K site-directed mutagenesis, the mutant enzyme is highly resistant to vanadate, but shows only slightly reduced sensitivity to bisdioxopiperazine compared to wild-type enzyme, reduced DNA hyperstimulation and DNA passage activity compared to the wild-type enzyme compared to the wild-type enzyme Homo sapiens
5.6.2.2 R162Q site-directed mutagenesis, the mutant enzyme is highly resistant to vanadate, the mutant shows no DNA hyperstimulation, nearly no ATPase activity, and reduced DNA passage activity and DNA hyperstimulation compared to the wild-type enzyme Homo sapiens
5.6.2.2 Y165S site-directed mutagenesis, the mutant enzyme is highly resistant to vanadate, the mutant shows no DNA hyperstimulation, nearly no ATPase activity, and highly reduced DNA passage activity and DNA hyperstimulation compared to the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.6.2.2 bisdioxopiperazine inhibition of wild-type enzyme and mutant R162K, inhibition mechanism Homo sapiens
5.6.2.2 vanadate inhibition of wild-type enzyme, no inhibition of mutant R162K, R162Q and Y165S, inhibition mechanism Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.2.2 0.21
-
 DNA pH 7.7, 37°C, DNA passage, mutant R162Q Homo sapiens
5.6.2.2 0.3
-
 DNA pH 7.7, 37°C, DNA passage, mutant Y165S Homo sapiens
5.6.2.2 0.39
-
 DNA pH 7.7, 37°C, DNA passage, wild-type enzyme Homo sapiens
5.6.2.2 0.55
-
 DNA pH 7.7, 37°C, DNA passage, mutant L169I Homo sapiens
5.6.2.2 0.61
-
 DNA pH 7.7, 37°C, DNA passage, mutant R162K Homo sapiens
5.6.2.2 0.94
-
 DNA pH 7.7, 37°C, DNA passage, mutant L169F Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.2 KCl required for DNA passage activity Homo sapiens
5.6.2.2 Mg2+ required for ATPase and DNA passage activities Homo sapiens
5.6.2.2 NaCl required for DNA passage activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.2 Homo sapiens
-
 isozyme alpha
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.6.2.2 additional information
-
 DNA hyperstimulation rates and ATPase activities of wild-type and mutant enzymes, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.2 dsDNA + ATP + H2O passage of dsDNA Homo sapiens ?
-
 ?
5.6.2.2 additional information the enzyme has intrinsic ATPase activity Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.6.2.2 Topoisomerase II
-
 Homo sapiens
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 37
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.2.2 0.6
-
 DNA pH 7.7, 37°C, DNA passage, mutant Y165S Homo sapiens
5.6.2.2 1.24
-
 DNA pH 7.7, 37°C, DNA passage, mutant R162Q Homo sapiens
5.6.2.2 1.65
-
 DNA pH 7.7, 37°C, DNA passage, mutant L169F Homo sapiens
5.6.2.2 1.8
-
 DNA pH 7.7, 37°C, DNA passage, mutant R162K Homo sapiens
5.6.2.2 3.33
-
 DNA pH 7.7, 37°C, DNA passage, mutant L169I Homo sapiens
5.6.2.2 3.38
-
 DNA pH 7.7, 37°C, DNA passage, wild-type enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6.2.2 7.5
-
 ATPase assay at Homo sapiens
5.6.2.2 7.7
-
 DNA passage assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
5.6.2.2 ATP
-
 Homo sapiens