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Biol Chem ; 386(11): 1105-14, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16307476

ABSTRACT

The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) by guanine nucleotide-binding proteins (GNBPs) is a fundamental enzyme reaction in living cells that acts as an important timer in a variety of biological processes. This reaction is intrinsically slow but can be stimulated by GTPase-activating proteins (GAPs) by several orders of magnitude. In the present study, we synthesized and characterized a new fluorescent nucleotide, 2'(3')-O-(N-ethylcarbamoyl-(5''-carboxytetramethylrhodamine) amide)-GTP, or tamraGTP, which is sensitive towards conformational changes of certain GNBPs induced by GTP hydrolysis. Unlike other fluorescent nucleotides, tamra-GTP allows real-time monitoring of the kinetics of the intrinsic and GAP-catalyzed GTP hydrolysis reactions of small GNBPs from the Rho family.


Subject(s)
GTP-Binding Proteins/chemistry , Guanosine Triphosphate/analogs & derivatives , Binding Sites , Fluorescent Dyes/chemical synthesis , Fluorescent Dyes/chemistry , GTP Phosphohydrolases/metabolism , GTP-Binding Proteins/metabolism , Guanosine Triphosphate/chemical synthesis , Guanosine Triphosphate/chemistry , Hydrolysis , Kinetics , Models, Molecular , rac1 GTP-Binding Protein/chemistry , rac1 GTP-Binding Protein/metabolism , rho GTP-Binding Proteins/metabolism
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