title: Monitoring ATP hydrolysis and ATPase inhibitor screening using (1)H NMR.
abstract: We present a versatile method to characterize ATPase and kinase activities and discover new inhibitors of these proteins. The proton NMR-based assay directly monitors ATP turnover and is easy to implement, requires no additional reagents and can potentially be applied to GTP. We validated the method's accuracy, applied it to the monitoring of ATP turnover by actin and to the screening of ATPase inhibitors, and showed that it is also applicable for the monitoring of GTP hydrolysis.
authors.affiliation: Department of Chemistry, Dartmouth College, Hanover 03755, USA. maria.pellegrini@dartmouth.edu dale.f.mierke@dartmouth.edu.
authors.forename: Bingqian
authors.initials: B
authors.lastname: Guo
authors.forename: Pinar S
authors.initials: PS
authors.lastname: Gurel
authors.forename: Rui
authors.initials: R
authors.lastname: Shu
authors.forename: Henry N
authors.initials: HN
authors.lastname: Higgs
authors.forename: Maria
authors.initials: M
authors.lastname: Pellegrini
authors.forename: Dale F
authors.initials: DF
authors.lastname: Mierke
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy
chemical_list: D004791:Enzyme Inhibitors; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases