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• W4230483849 endingPage "1464" @default.
• W4230483849 startingPage "1460" @default.
• W4230483849 abstract "Type IIA topos (topoisomerases) catalyse topological conversions of DNA through the passage of one double strand through a transient break in another. In the case of the archetypal enzyme, DNA gyrase, it has always been apparent that the enzyme couples the free energy of ATP hydrolysis to the introduction of negative supercoiling, and the structural details of this process are now becoming clearer. The homologous type IIA enzymes such as topo IV and eukaryotic topo II also require ATP and it has more recently been shown that the energy of hydrolysis is coupled to a reduction of supercoiling or catenation (linking) beyond equilibrium. The mechanism behind this effect is less clear. We review the energy coupling process in both classes of enzyme and describe recent mechanistic and structural work on gyrase that addresses the mechanism of energy coupling." @default.
• W4230483849 created "2022-05-11" @default.
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• W4230483849 date "2005-10-26" @default.
• W4230483849 modified "2023-09-27" @default.
• W4230483849 title "Coupling ATP hydrolysis to DNA strand passage in type IIA DNA topoisomerases" @default.
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• W4230483849 doi "https://doi.org/10.1042/bst0331460" @default.
• W4230483849 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16246146" @default.
• W4230483849 hasPublicationYear "2005" @default.
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