Literature summary for 5.6.2.2 extracted from

Declais, A.C.; Marsault, J.; Confalonieri, F.; de La Tour, C.B.; Duguet, M.
Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling (2000), J. Biol. Chem., 275, 19498-19504.

Search for more literature for 5.6.2.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sulfolobus acidocaldarius

Organism

Organism	UniProt	Comment	Textmining
Sulfolobus acidocaldarius	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	helicase activity for both the N-terminal domain and the full-length reverse gyrase	Sulfolobus acidocaldarius	?	-	?
negatively supercoiled plasmid DNA + ATP + H2O	the full-length recombinant enzyme sustains ATP-dependent positive supercoiling. The C-terminal half of Sulfolobus reverse gyrase, expressed in Escherichia coli, exhibits a topoisomerase I activity, independent of the presence of ATP and specific of negative supercoils.The N-terminal domain does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, reminiscent of a protein motor	Sulfolobus acidocaldarius	negatively supercoiled plasmid DNA + ADP + phosphate	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
75	-	assay at	Sulfolobus acidocaldarius

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Sulfolobus acidocaldarius

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Release 2023.1 (January 2023)