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Literature summary for 5.6.2.1 extracted from

  • Goulaouic, H.; Roulon, T.; Flamand, O.; Grondard, L.; Lavelle, F.; Riou, J.F.
    Purification and characterization of human DNA topoisomerase IIIalpha (1999), Nucleic Acids Res., 27, 2443-2450.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.1

Activating Compound

Activating Compound Comment Organism Structure
glycerol high concentrations increase the efficiency of the DNA relaxation reaction Homo sapiens

Protein Variants

Protein Variants Comment Organism
Y337F mutant enzyme is still able to bind single-stranded DNA but is unable to cleave the DNA substrate because of the absence of the active Tyr337 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
KCl above 100 mM Homo sapiens
NaCl above 100 mM Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on, low concentrations of MgCl2 are sufficient to obtain efficient catalysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
negatively supercoiled DNA the enzyme relaxes negatively supercoiled DNA in a distributive manner, leading to the total disappearance of the initial substrate and the appearance of intermediate topoisomers. The enzyme is able to cleave a single stranded oligonucleotide to bind covalently to the 5‘-end of cleaved DNA. The consensus sequence for DNA cleavage is CANNN-/- Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
hTopo IIIalpha
-
 Homo sapiens
topoisomerase IIIalpha
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37 45
-
 Homo sapiens