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. Author manuscript; available in PMC: 2011 Jan 1.
Published in final edited form as: Chem Biol Drug Des. 2010 Jan;75(1):51–67. doi: 10.1111/j.1747-0285.2009.00914.x

Figure 4.

Figure 4

Evaluation of amide 3 as an alternative substrate and inhibitor of ScPFTase. (A) Reaction between N-dansyl-GCVIA and FPP or amide 3 catalyzed by ScPFTase monitored by fluorescence spectroscopy. (a) Kinetic data using FPP as a substrate. (b) Kinetic data using amide 3 as a substrate. Fluorescence was monitored at 30°C by excitation at 340 nm and emission at 505 nm. (B) .Inhibition of ScPFTase-catalyzed farnesylation of N-dansyl-GCVIA by amide 3. Reactions contained 2.0 μM FPP, 2.0 μM N-dansyl-GCVIA and 3 at varying concentrations and were monitored using a continuous spectrofluorometric assay. Each point is the average of 2-3 determinations with the error bars indicating the standard error for each measurement.