Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. II. Structural elucidation of pepticinnamin E

K Shiomi; H Yang; J Inokoshi; D Van der Pyl; A Nakagawa; H Takeshima; S Omura

doi:10.7164/antibiotics.46.229

Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. II. Structural elucidation of pepticinnamin E

J Antibiot (Tokyo). 1993 Feb;46(2):229-34. doi: 10.7164/antibiotics.46.229.

Authors

K Shiomi¹, H Yang, J Inokoshi, D Van der Pyl, A Nakagawa, H Takeshima, S Omura

Affiliation

¹ Research Center for Biological Function, Kitasato Institute, Tokyo, Japan.

PMID: 8468236
DOI: 10.7164/antibiotics.46.229

Abstract

Structure of novel farnesyl transferase inhibitor, pepticinnamin E, is elucidated by NMR study. Pepticinnamin E is composed of five amino acids and o-pentenylcinnamic acid, having a molecular weight of 907. C-terminal glycylserine of the compounds is in the cyclized diketopiperazine form.

MeSH terms

Actinomyces / metabolism*
Alkyl and Aryl Transferases*
Amino Acid Sequence
Enzyme Inhibitors / chemistry
Molecular Sequence Data
Molecular Weight
Oligopeptides / chemistry*
Transferases / antagonists & inhibitors*

Substances

Enzyme Inhibitors
Oligopeptides
pepticinnamin E
Transferases
Alkyl and Aryl Transferases
p21(ras) farnesyl-protein transferase