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Literature summary for 5.6.2.1 extracted from

  • Rajan, R.; Osterman, A.K.; Gast, A.T.; Mondragón, A.
    Biochemical characterization of the topoisomerase domain of Methanopyrus kandleri topoisomerase V (2014), J. Biol. Chem., 289, 28898-28909.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.1

Protein Variants

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

Organism UniProt Comment Textmining
Methanopyrus kandleri
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-
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Purification (Commentary)

Purification (Comment) Organism
-
 Methanopyrus kandleri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
negatively supercoiled DNA
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 Methanopyrus kandleri relaxed DNA
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 ?

Synonyms

Synonyms Comment Organism
topoisomerase V
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 Methanopyrus kandleri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
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 assay at Methanopyrus kandleri