PMID:22064072

Citation	Salvarelli, E, Krupka, M, Rivas, G, Vicente, M and Mingorance, J (2011) Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ. FEBS Lett. 585:3880-3
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.
Links	PubMed Online version:10.1016/j.febslet.2011.10.046
Keywords	Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding, Competitive; Catalytic Domain; Cell Division; Cytoskeletal Proteins/antagonists & inhibitors; Cytoskeletal Proteins/chemistry; Cytoskeletal Proteins/metabolism; Enzyme Inhibitors/metabolism; Enzyme Inhibitors/pharmacology; Escherichia coli/cytology; Escherichia coli/metabolism; GTP Phosphohydrolases/metabolism; Guanosine Diphosphate/metabolism; Guanosine Diphosphate/pharmacology; Guanosine Triphosphate/analogs & derivatives; Guanosine Triphosphate/metabolism; Guanosine Triphosphate/pharmacology; Hydrolysis; Kinetics
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