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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Role of the divalent cation in topoisomerase II mediated reactions.

The effects of magnesium ions on interactions between Drosophila melanogaster topoisomerase II and its substrates were assessed by a number of kinetic and binding assays. Results indicated that the divalent cation plays two distinct functions in promoting enzyme-substrate interactions. One class of magnesium ions participates directly in enzyme-mediated DNA cleavage reactions. A second class of magnesium ions participates directly in topoisomerase II mediated ATPase reactions and functions by providing the enzyme with a magnesium-ATP substrate. In contrast, the divalent cation did not affect the quaternary structure of the enzyme, was not required for the site-specific binding of topoisomerase II to DNA, and did not affect the enzyme's ability to discern the topological state of its nucleic acid substrate.[1]


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