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. Author manuscript; available in PMC: 2026 Jan 7.
Published in final edited form as: Biochemistry. 2024 Dec 9;64(1):138–155. doi: 10.1021/acs.biochem.4c00558

Figure 1: General schematic of prenylation, enzyme function, and comparison of probes.

Figure 1:

A) General schematic of the farnesylation and geranylgeranylation type I, two subtypes of prenylation. B) Comparisons of the prenylation probes used in this study compared to the native substrates, purple line shows length of FPP, blue line shows length of GGPP. C) Computational modeling showing the docking of C10AlkOPP (carbon; orange), C15AlkOPP (carbon; purple), C15hAlkOPP (carbon; yellow) and C20AlkOPP (carbon; green) into the three prenylation enzyme binding pockets superimposed on the native substrate FPP (carbon; pink) or GGPP (carbon; blue) respectively. Left FTase binding cavity (1JCR, red mesh), middle GGTase I binding cavity (1TNO, blue mesh), right GGTase II binding cavity (3DST, green mesh). For all ligands, oxygen is red, and phosphorus is orange.