A CEMBRANOLIDE DITERPENE FARNESYL PROTEIN TRANSFERASE INHIBITOR FROM THE MARINE SOFT CORAL LOBOPHYTUM CRISTAGALLI.

Authors

S. J. Coval, Schering Plough Research Institute
R. W. Patton, Florida Atlantic University
J. M. Petrin, Florida Atlantic University
L. James, Florida Atlantic University
M. L. Rothofsky, Florida Atlantic University
S. L. Lin, Florida Atlantic University
Mahesh Patel, Florida Atlantic University
John K. Reed, Florida Atlantic University
A. T. McPhail, Duke University
W. R. Bishop, Duke University

Author Type

Faculty

Document Type

Article

Abstract

A previously described cembranolide diterpene from Lobophytum cristagalli was identified as a potent (lC so 0.15 11M) inhibitor of farnesyl protein transferase (FPT). The compound showed selectivity for FPT as compared to the closely related enzyme geranylgeranyl protein transferase-I (ICso 5.3 11M). Kinetic evaluation suggests that this compound competes with the protein/peptide farnesyl acceptor substrate, and not with farnesyl pyrophosphate for inhibition of FPT.

DOI

10.1016/0960-894X(96)00142-4 (doi)

Publication Date

1996

Comments

Florida Atlantic University. Harbor Branch Oceanographic Institute contribution #1131.

Recommended Citation

This manuscript is an author version with the final publication available at http://www.sciencedirect.com/science/journal/0960894X and may be cited as: Coval, S. J., Patton, R. W., Petrin, J. M., James, L., Rothofsky, M. L., Lin, S. L., Patel, M., Reed, J. K., McPhail, A. T., & Bishop, W. R. (1996). A cembranolide diterpene farnesyl protein transferase inhibitor from the marine soft coral Lobophytum cristagalli. Bioorganic & Medicinal Chemistry Letters, 6(7), 909-912. doi:10.1016/0960-894X(96)00142-4