title: Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ.
abstract: We have analyzed the substrate kinetics of the GTPase activity of FtsZ and the effects of two different GTPase inhibitors, GDP and the slowly hydrolyzable GTP analogue GMPCPP. In the absence of inhibitors the GTPase activity follows simple Michaelis-Menten kinetics, and both GDP and GMPCPP inhibited the activity in a competitive manner. These results indicate that the GTPase active sites in FtsZ filaments are independent of each other, a feature relevant to elucidate the role of GTP hydrolysis in FtsZ function and cell division.
authors: Servicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, Madrid, Spain.
authors: Estefanía
authors: E
authors: Salvarelli
authors: Marcin
authors: M
authors: Krupka
authors: Germán
authors: G
authors: Rivas
authors: Miguel
authors: M
authors: Vicente
authors: Jesús
authors: J
authors: Mingorance
mesh_terms: D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D001667:Binding, Competitive; D020134:Catalytic Domain; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000378:metabolism / Q000494:pharmacology; D004926:Escherichia coli / Q000166:cytology* / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D004791:Enzyme Inhibitors; C071525:FtsZ protein, Bacteria; D006153:Guanosine Diphosphate; C004805:5'-guanylylmethylenebisphosphonate; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases