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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Monitoring the real-time kinetics of the hydrolysis reaction of guanine nucleotide-binding proteins

Alexander Eberth1 / Radovan Dvorsky2 / Christian F.W. Becker3 / Andrea Beste4 / Roger S. Goody5 / Mohammad Reza Ahmadian6







Corresponding author

Citation Information: Biological Chemistry. Volume 386, Issue 11, Pages 1105–1114, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2005.127, November 2005

Publication History

July 7, 2005
August 30, 2005
Published Online:


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.

Keywords: fluorescence reporter; GTPase; GTPase-activating protein; GTP hydrolysis; guanine nucleotide-binding protein; rhodamine; spectroscopy

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