Protein Variants | Comment | Organism |
---|---|---|
E215A | mutant activity with the mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) is active over a wider range of pH values, compared with wild-type enzyme. Mutant activity with the mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) is active over a wider range of pH values, compared with wild-type enzyme | Methanopyrus kandleri |
E215H | mutant enzyme is active over a wider range of pH values, compared with wild-type enzyme, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
E215Q | mutant enzyme is active over a wider range of pH values, compared with wild-type enzyme, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
E215R | mutant enzyme is active over a wider range of pH values, compared with wild-type enzyme, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
H200A | mutant enzyme is slightly less active than wild type enzyme, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
H200E | mutant has low but detectable DNA relaxation activity at pH 5, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
H200N | mutant enzyme is slightly less active than wild type enzyme, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
H200Q | mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
H200R | mutant enzyme shows relaxation activity over a pH range similar to the wild-type enzyme. In the Topo-78 backbone (an N-terminal 78-kDa fragment of Topo-V), qualitatively, H200R is as active as the wild type | Methanopyrus kandleri |
K128R | mutant enzyme shows very minimal activity at pH 8 | Methanopyrus kandleri |
K218Q | the mutant is inactive in all of the pH conditions tested, mutation in the Topo-78 fragment (an N-terminal 78-kDa fragment of Topo-V) | Methanopyrus kandleri |
R131A | mutant shows no detectable DNA relaxation activity, mutations in Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) or in Topo-78 fragment (an N-terminal 78-kDa fragment of Topo-V) | Methanopyrus kandleri |
R131K | conservative substitution that retains both the electrostatic and acid/base properties, except for the loss of the bidentate coordination possible through the guanidinium group of the arginine. Whereas the R131K mutant is purified successfully in the Topo-44 backbone, it results in degradation when expressed in the Topo-78 backbone | Methanopyrus kandleri |
R144A | mutant enzyme shows no activity, mutation in Topo-78 fragment (an N-terminal 78-kDa fragment of Topo-V) | Methanopyrus kandleri |
T226F | the mutation abolishes activity at all pH values in T44Y226F and shows only minimal activity at pH 8, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
Y226F | mutation abolishes DNA binding, mutation in the Topo-44 fragment (an N-terminal 44-kDa fragment of Topo-V) | Methanopyrus kandleri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanopyrus kandleri | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Methanopyrus kandleri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
negatively supercoiled DNA | - |
Methanopyrus kandleri | relaxed DNA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
topoisomerase V | - |
Methanopyrus kandleri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
assay at | Methanopyrus kandleri |