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Literature summary for 5.6.2.2 extracted from

  • Valenti, A.; Perugino, G.; D'Amaro, A.; Cacace, A.; Napoli, A.; Rossi, M.; Ciaramella, M.
    Dissection of reverse gyrase activities: insight into the evolution of a thermostable molecular machine (2008), Nucleic Acids Res., 36, 4587-4597.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

General Stability

General Stability Organism
the activity of TopR1 and the two separate domains is very sensitive to repeated freezing, excessive dilution and prolonged storage, due to protein degradation Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-value for ATP is 77.1 mM Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus P2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme induces positive supercoiling into DNA molecules in an ATP-dependent reaction. The isolated ATPase and topoisomerase domains of reverse gyrase form specific physical interactions, retain their own DNA binding and enzymatic activities, and when combined cooperate to achieve the unique ATP-dependent positive supercoiling activity Saccharolobus solfataricus ?
-
 ?
additional information the enzyme induces positive supercoiling into DNA molecules in an ATP-dependent reaction. The isolated ATPase and topoisomerase domains of reverse gyrase form specific physical interactions, retain their own DNA binding and enzymatic activities, and when combined cooperate to achieve the unique ATP-dependent positive supercoiling activity Saccharolobus solfataricus P2 ?
-
 ?

Synonyms

Synonyms Comment Organism
Reverse gyrase
-
 Saccharolobus solfataricus
TopR1
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 assay at Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover number for ATP hydrolysis is 2.55/s Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Saccharolobus solfataricus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information kcat/Km for ATP hydrolysis is 0.033 mM/s Saccharolobus solfataricus