New cyclodepsipeptides, enniatins D, E and F produced by Fusarium sp. FO-1305.

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Author(s)

    • TOMODA HIROSHI
    • Research Center for Biological Function, The Kitasato Institute
    • NISHIDA HIROYUKI
    • Research Center for Biological Function, The Kitasato Institute|Present address: Pfizer Central Research, Nagoya, Pfizer Pharmaceuticals Inc.
    • HUANG XIN-HUI
    • Research Center for Biological Function, The Kitasato Institute
    • MASUMA ROKURO
    • Research Center for Biological Function, The Kitasato Institute
    • KIM YOUNG KOOK
    • Research Center for Biological Function, The Kitasato Institute
    • OMURA SATOSHI
    • Research Center for Biological Function, The Kitasato Institute

Abstract

New cyclodepsipeptides named enniatins D, E and F were isolated from the culture broth of <i>Fusarium</i> sp. FO-1305 as inhibitors of acyl-CoA: cholesterol acyltransferase (ACAT). The respective structures of enniatins D, E and F were determined to be cyclo[D-α-hydroxyisovaleryl(D-Hiv)-L-<i>N</i>-methylleucinyl (L-Me-Leu)-D-Hiv-L-<i>N</i>-methylvalinyl(L-Me-Val)-D-Hiv-L-Me-Val], a mixture of cyclo[D-Hiv-L-Me-Leu-D-Hiv-L-<i>N</i>-methylisoleuciny (L-Me-He-D)-D-Hiv-L-Me-Val], and cyclo(D-Hiv-L-Me-Ile-D-Hiv-L-Me-Leu-o-Hiv-L-Me-Val), and cyclo (D-Hiv-L-Me-Leu-D-Hiv-L-Me-Ile-D-Hiv-L-Me-Ile) by spectral analyses and chemical degradation. The IC<sub>50</sub> values of enniatins D, E and F for ACAT activity in an enzyme assay using rat liver microsomes were calculated to be 87, 57 and 40μM, respectively.

Journal

  • The Journal of Antibiotics

    The Journal of Antibiotics 45(8), 1207-1215, 1992

    JAPAN ANTIBIOTICS RESEARCH ASSOCIATION

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