Pholipeptin, a Novel Cyclic Lipoundecapeptide fromPseudomonas fluorescens.
An inhibitor of phosphatidylinositol-specific phospholipase C (PI-PLC), pholipeptin (1), was purified from the culture broth of Pseudomonas sp. by solvent extraction and column chromatography. Acid hydrolysis of 1 gave Leu, Ile, Ser, Thr, and Asp moieties. Although 1 was a peptide compound, fragmentation by mild hydrolysis was not accomplished under any conditions. So, we performed the structure elucidation using various 2D NMR techniques. In the NMR studies, the addition of a small amount of trifluoroacetic acid gave relatively sharp and resolved signals, such that the structure of this novel cyclic lipodepsipeptide consisting of 11 amino acids and a 3-hydroxydecanoic acid moiety could be determined. Chirality of the constituent amino acids was analyzed by chiral HPLC, but two Asp residues could not be distinguished because they were contained as a racemic mixture. Finally, their chiralities were determined by NMR analysis of (13)C-labeled 1 into which [L-(13)C]Asp had been biosynthetically incorporated.
Ui
Hideaki
H
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223, Japan, Institute of Bioorganic Chemistry, 3-34-17 Ida, Nakahara-ku, Kawasaki 211, Japan, and Institute of Microbial Chemistry, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo 141, Japan.
Miyake
Toshiaki
T
Iinuma
Hironobu
H
Imoto
Masaya
M
Naganawa
Hiroshi
H
Hattori
Seiko
S
Hamada
Masa
M
Takeuchi
Tomio
T
Umezawa
Sumio
S
Umezawa
Kazuo
K