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Literature summary for 5.6.2.2 extracted from

  • Krah, R.; O'Dea, M.H.; Gellert, M.
    Reverse gyrase from Methanopyrus kandleri. Reconstitution of an active extremozyme from its two recombinant subunits (1997), J. Biol. Chem., 272, 13986-13990.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. Reconstitution of the heterodimeric active reverse gyrase from the two recombinant proteins overexpressed in Escherichia coli and purification. Subunit RgyB has a DNA-dependent ATPase activity at high temperature (80 °C) and is independent of the presence of subunit RgyA. Subunit RgyA alone has no detectable activity. The addition of subunit RgyA to subunit RgyB reconstitutes positive supercoiling activity Methanopyrus kandleri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
1 * 138000 + 1 * 43000, the 138000 Da subunit is involved in the hydrolysis of ATP (RgyB) and the 43000 Da subunit forms the covalent complex with DNA during the topoisomerase reaction (RgyA) Methanopyrus kandleri
138000
-
1 * 138000 + 1 * 43000, the 138000 Da subunit is involved in the hydrolysis of ATP (RgyB) and the 43000 Da subunit forms the covalent complex with DNA during the topoisomerase reaction (RgyA) Methanopyrus kandleri

Organism

Organism UniProt Comment Textmining
Methanopyrus kandleri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanopyrus kandleri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information reconstitution of the heterodimeric active reverse gyrase from the two recombinant proteins overexpressed in Escherichia coli and purification. Subunit RgyB has a DNA-dependent ATPase activity at high temperature (80 °C) and is independent of the presence of subunit RgyA. Subunit RgyA alone has no detectable activity. The addition of subunit RgyA to subunit RgyB reconstitutes positive supercoiling activity Methanopyrus kandleri ?
-
?
negatively supercoiled DNA + ATP + H2O
-
Methanopyrus kandleri positively supercoiled DNA + ADP + phosphate
-
?
relaxed DNA + ATP + H2O
-
Methanopyrus kandleri positively supercoiled DNA + ADP + phosphate
-
?

Subunits

Subunits Comment Organism
heterodimer 1 * 138000 + 1 * 43000, the 138000 Da subunit is involved in the hydrolysis of ATP (RgyB) and the 43000 Da subunit forms the covalent complex with DNA during the topoisomerase reaction (RgyA) Methanopyrus kandleri

Synonyms

Synonyms Comment Organism
ATP-dependent type I 5'-topoisomerase
-
Methanopyrus kandleri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
assay at Methanopyrus kandleri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Methanopyrus kandleri