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Literature summary for 5.6.2.1 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
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Protein Variants

Protein Variants Comment Organism
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
N726S mutant enzyme is resistant to camptothecin Saccharomyces cerevisiae
Y727F inactive mutant enzyme Saccharomyces cerevisiae

Inhibitors

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

Metals/Ions

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

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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