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Literature summary for 5.6.2.1 extracted from

  • Colley, W.C.; van der Merwe, M.; Vance, J.R.; Burgin, A.B., Jr.; Bjornsti, M.A.
    Substitution of conserved residues within the active site alters the cleavage religation equilibrium of DNA topoisomerase I (2004), J. Biol. Chem., 279, 54069-54078.
    View publication on PubMed
Search for more literature for 5.6.2.1

Protein Variants

Protein Variants Comment Organism
N726D self-poisoning phenotype, reduced rate of DNA religation relative to wild-type enzyme, affinity for DNA is reduced about 2.5fold relative to that observed for wild-type Top1p at 50 or 75 mM KCl Saccharomyces cerevisiae
N726F specific activity is about 5fold lower than that of wild-type enzyme, self-poisoning phenotype, mutation enhances the kinetics of DNA cleavage Saccharomyces cerevisiae
N726H self-poisoning phenotype, specific activity is about 5fold lower than that of wild-type enzyme, binding of DNA increases from 2.5fold at 50 mM KCl to 4fold at 100 mM KCl, 10fold increase in DNA cleavage activity Saccharomyces cerevisiae
N726K camptothecin resistance of cells expressing the mutant enzyme Saccharomyces cerevisiae
N726Q camptothecin resistance of cells expressing the mutant enzyme Saccharomyces cerevisiae
N726Y mutation enhances the kinetics of DNA cleavage Saccharomyces cerevisiae
T722A self-poisoning phenotype, reduced rate of DNA religation relative to wild-type enzyme, specific activity of the mutant enzyme is slightly decreased, however protein binding of DNA and rates of enzyme-catalyzed Saccharomyces cerevisiae
T722A/N726H specific activity is about 5fold lower than that of wild-type enzyme, N726H mutation potentiates the cytotoxic activity of T722A, increase in DNA cleavage activity Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Top1p
-
 Saccharomyces cerevisiae