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Many ATP- or GTP-binding enzymes display hydrolysis of the bound nucleotide at a rate that prevents close investigation of their triphosphate-bound state. To circumvent this problem one often uses modified nucleotides that are resistant to such enzymatic hydrolysis or that are hydrolized at much smaller rates than their natural NTP counterparts. These analogs allow trapping of kinases, GTPases, motor proteins, and other NTP-binding enzymes in their triphosphate bound state and therefore, are widely used as inhibitors[1], in purinoceptor research[2],[3], for investigation of microtubules[4],[5], for co-crystallization[6], for kinetic assays, or as biochemical probes. Jena Bioscience offers the complete portfolio of nucleotide analogs with a modified phosphate moiety that are resistant to hydrolysis. Either
For example, a GTP analog in which a bridging oxygen in between phosphates β and γ is replaced by a methyleno-group would be termed GppCp (Guanosine-β,γ-methyleno-triphosphate) whereas a GTP with a sulfur-substitution at phosphate γ is typically called GTPγS, please see the table below.
To browse our whole portfolio of non-hydrolyzable nucleotides please click here:
www.jenabioscience.com/cms/en/1/browse/227/
Nucleotide analogs not on stock may be available as custom synthesis, just send us an e-mail at nucleotides@jenabioscience.com with any questions you may have!
Selected references:
[1] Leoni et al. (2000) Nucleotide requirements for the in vitro activation of the apoptosis protein-activating factor-1-mediated caspase pathway. J. Biol. Chem. 275 (1):29. [2] Inscho (2001) Renal microvascular effects of P2 receptor stimulation. Clin. Exp. Pharm. Phys. 28:322. [3] Dunn (2000) Fertility: Purinergic receptors and the male contraceptive pill. Curr. Biol. 10 (8):R305. [4] Salmon et al. (1997) How tubulin subunits are lost from the shortening ends of microtubules. J. Struct. Biol. 118:107. [5] Dye et al. (1996) Assembly of microtubules from tubulin bearing the nonhydrolyzable guanosine triphosphate analogue GMPPCP [Guanylyl-5'-(β,γ-Methylenediphosphonate)]: variability of growth rates and the hydrolysis of GTP. Biochem. 35 (45):14331. [6] Vértessy et al. (2007) Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins. Nucleic Acids Research 35 (2):495. |
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