Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. II. Structural elucidation of pepticinnamin E.
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.
Shiomi
K
K
Research Center for Biological Function, Kitasato Institute, Tokyo, Japan.
Yang
H
H
Inokoshi
J
J
Van der Pyl
D
D
Nakagawa
A
A
Takeshima
H
H
Omura
S
S
D000190:Actinomyces / Q000378:metabolism*; D019883:Alkyl and Aryl Transferases; D000595:Amino Acid Sequence; D004791:Enzyme Inhibitors / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry*; D014166:Transferases / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D009842:Oligopeptides; C080552:pepticinnamin E; D014166:Transferases; D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase