Synthesis and evaluation of benzophenone-based photoaffinity labeling analogs of prenyl pyrophosphates containing stable amide linkages
Compounds 1a and 1b inhibit farnesyl protein transferase (K1 = 6000 nM and 700 nM). Irradiation of [32P]-1b in the presence of farnesyl and geranylgeranyl protein transferases results in preferential labeling of the β-subunits of these enzymes.
References (28)
- et al.
Chemistry and Biology
(1995) - et al.
Cell
(1994) - et al.
Tetrahedron Lett.
(1996) - et al.
Biochem. Biophys. Res. Comm.
(1991) - et al.
J. Biol. Chem.
(1995) - et al.
Biochem. Biophys. Res. Comm.
(1997) - et al.
Tetrahedron
(1996) - et al.
J. Biol. Chem.
(1994) - et al.
Ann. Rev. Biochem.
(1996) Tetrahedron
(1995)
J. Org. Chem.
Biochemistry
Biochemistry
Synthesis
Cited by (31)
The chaperone protein smggds interacts with small gtpases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif
2014, Journal of Biological ChemistryCitation Excerpt :The [M + 2H]2+ values for ESI-MS were 1079.64 (calculated) and 1079.73 (found). Synthesis followed the same prenylation conditions as described above using C10-meta-Bp-Br (22.8 mg, 53.5 μmol, 5 eq) that was prepared as previously described (34–37). This reaction yielded 3.4 mg (14%) of the desired alkylated peptide.
Natural rubber (NR) biosynthesis: Perspectives from polymer chemistry
2014, Chemistry, Manufacture and Applications of Natural RubberFluorescent substrate analog for monitoring chain elongation by undecaprenyl pyrophosphate synthase in real time
2011, Analytical BiochemistryCitation Excerpt :Wild-type and D26A and S83A5 mutant UPPS were purified as previously described [15,16]. MANT-O-GPP was synthesized according to reported procedures [17–20] with modifications as shown in Supplementary data. Radiolabeled [14C]IPP (55 mCi/mmol) was purchased from Amersham Pharmacia Biotech.
Synthesis of a-factor peptide from Saccharomyces cerevisiae and photoactive analogues via Fmoc solid phase methodology
2011, Bioorganic and Medicinal ChemistryCitation Excerpt :Given the membrane bound nature of Ste3p, the a-factor receptor, photoaffinity labeling is an attractive method to probe the interaction between the protein and the pheromone. Several laboratories have developed analogues of the farnesyl moiety that incorporate photoactivatable groups into the isoprenoids themselves, allowing specific interactions between prenyl groups and their cognate protein receptors to be studied; those molecules include diazotrifluropropionates8–16, benzophenones17–27 and aryl azides.28,29 Thus, we envisioned that a-factor analogues suitably functionalized with photoactive farnesyl groups would be useful for this purpose and accordingly, we sought to prepare such molecules via solid-phase peptide synthetic methods.
A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes
2009, Bioorganic and Medicinal Chemistry