Protein Variants | Comment | Organism |
---|---|---|
additional information | dissociation constants obtained for binding of wild-type EcTOP1, R169A, R173A and Y177S mutant enzymes to 3'-labeled 59 base hairpin oligonucleotide substrates, Oligo C, Oligo A and Oligo G, overview | Escherichia coli |
R169 | site-directed mutagenesis, the mutant shows reduced DNA cleavage and relaxation activity compared to the wild-type enzyme, the mutation to alanine changesd the selectivity of the enzyme for the base at the -4 position from a cytosine to an adenine | Escherichia coli |
R173A | site-directed mutagenesis, the mutant displays similar sequence selectivity as the wild-type enzyme, but weaker cleavage and relaxation activity | Escherichia coli |
Y177A | site-directed mutagenesis, inactive mutant | Escherichia coli |
Y177S | site-directed mutagenesis, inactive mutant | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | dissociation constants obtained for binding of wild-type EcTOP1, R169A, R173A and Y177S mutant enzymes to 3'-labeled 59 base hairpin oligonucleotide substrates, Oligo C, Oligo A and Oligo G, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | cleavage of 556 base single-stranded DNA substrate supercoiled pBAD/thio plasmid, and cleavage and religation of 59 base hairpin oligonucleotide substrates | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Topoisomerase I | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
additional information | residues R169, R173 and Y177 work together to interact with a cytosine base at the -4 position to facilitate DNA cleavage. R169 and R173 interact with the cytosine base at the -4 position via hydrogen bonds while the phenol ring of Y177 wedges between the bases at the -4 and the -5 position | Escherichia coli |