
doi: 10.1042/bst0380438
pmid: 20298198
Type II DNA topoisomerases catalyse changes in DNA topology in reactions coupled to the hydrolysis of ATP. In the case of DNA gyrase, which can introduce supercoils into DNA, the requirement for free energy is clear. However, the non-supercoiling type II enzymes carry out reactions that are apparently energetically favourable, so their requirement for ATP hydrolysis is not so obvious. It has been shown that many of these enzymes (the type IIA family) can simplify the topology of their DNA substrates to a level beyond that expected at equilibrium. Although this seems to explain their usage of ATP, we show that the free energies involved in topology simplification are very small (<0.2% of that available from ATP) and we argue that topology simplification may simply be an evolutionary relic.
Adenosine Triphosphate, DNA Topoisomerases, Type II, Hydrolysis, Humans, Nucleic Acid Conformation, DNA, Energy Metabolism, Models, Biological, Catalysis, Protein Binding
Adenosine Triphosphate, DNA Topoisomerases, Type II, Hydrolysis, Humans, Nucleic Acid Conformation, DNA, Energy Metabolism, Models, Biological, Catalysis, Protein Binding
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