Characterisation of the DNA-dependent ATPase activity of human DNA topoisomerase IIβ: mutation of Ser165 in the ATPase domain reduces the ATPase activity and abolishes the in vivo complementation ability

We report for the first time an analysis of the ATPase activity of human DNA topoisomerase (topo) IIβ. We show that topo IIβ is a DNA-dependent ATPase that appears to fit Michaelis–Menten kinetics. The ATPase activity is stimulated 44-fold by DNA. The k(cat) for ATP hydrolysis by human DNA topo IIβ...

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Pubblicato in:	Nucleic Acids Res
Autori principali:	West, Katherine L., Turnbull, Rosalind M., Willmore, Elaine, Lakey, Jeremy H., Austin, Caroline A.
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	Oxford University Press 2002
Soggetti:	Articles
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC140051/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12490710/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/gkf677
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