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Literature summary extracted from

  • Fertala, J.; Vance, J.R.; Pourquier, P.; Pommier, Y.; Bjornsti, M.A.
    Substitutions of Asn-726 in the active site of yeast DNA topoisomerase I define novel mechanisms of stabilizing the covalent enzyme-DNA intermediate (2000), J. Biol. Chem., 275, 15246-15253.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.1 N726D mutant enzyme is resistant to camptothecin, no appreciable decrease in catalytic activity, exhibits a distributive mode of plasmid DNA relaxation compared to a progressive mode of the wild-type enzyme. Activity of the mutant enzyme is optimal at 75-100 mM KCl, compared to 150 mM KCl for the wild-type enzyme Saccharomyces cerevisiae
5.6.2.1 N726S mutant enzyme is resistant to camptothecin Saccharomyces cerevisiae
5.6.2.1 Y727F inactive mutant enzyme Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.6.2.1 camptothecin inhibition of wild-type enzyme, no inhibition of mutant enzymes N726S and N726S Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.1 KCl maximal activity of wild-type enzyme at 150 mM, maximal activity of mutant enzyme N726D at 75-100 mM Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.1 Saccharomyces cerevisiae
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.1 additional information wild-type enzyme and mutant enzyme N726H exhibit a distinctively processive mode of plasmid relaxation, mutant enzyme N726D exhibits a distributive mode of plasmid DNA relaxation Saccharomyces cerevisiae ?
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