Discovery, producing organism and structure (1-3)
Pepticinnamins, consisting of 6 components, were isolated from a culture broth of the actinomycete strain OH-4652 and recognized as inhibitors of protein farnesyltransferase from an assay using a partially purified enzyme from human monocyte THP-1 (ATCC TIB 202). The structure of component E was elucidated. The stereochemistry of the amino acids was elucidated using chiral HPLC, with the exception of N-methyl-(2-chloro-3- hydroxy-4-methoxy)-phenylalanine. Its stereochemistry was revealed by total synthesis of the pepticinnamin E diastereomers (3).
Physical data (Pepticinnamin E)
White powder. C49H54N5O10Cl; mol wt 908.46. Sol. in DMSO, MeOH, EtOAc, CHCl3. Insol. in H2O, hexane.
Biological activity (1,4,5)
1) Specific protein farnesyltransferase inhibition
Protein farnesyltransferase catalyses a post-translational modification of ras p21 obligatory for cell transformation of the oncogene protein.
2) Kinetic analysis of protein farnesyltransferase inhibition by pepticinnamin E
Pepticinnamin E inhibits protein farnesyltransferase competitively with respect to ras p21 and noncompetitively with respect to farnesyl diphosphate (FPP).
1  S. Ōmura et al., J. Antibiot., 46, 222–228 (1993)
2.  K. Shiomi et al., J. Antibiot., 46, 229–234 (1993)
3. K. Hinterding et al., Angew. Chem. Int. Ed. Engl., 37, 1236–1239 (1998)
4.  H. Takeshima and S. Omura, Tanpakushitsu Kakusan Koso, 38, 1695–1703 (1993)
5.  S. Ōmura and H. Tomoda, Pure Appl. Chem., 66, 2267–2270 (1994).