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- W1973566996 abstract "Inositol phosphorylceramide synthase (IPC synthase) is an essential and unique enzyme in fungal sphingolipid biosynthesis and is the target of the cyclic nonadepsipeptide antibiotic aureobasidin A. As a first step towards understanding the mechanism of aureobasidin A inhibition, we developed a fluorometric HPLC assay for IPC synthase using the Saccharomyces cerevisiae enzyme and the fluorescent substrate analog 6‐[ N ‐(7‐nitro‐2,1,3‐benzoxadiazol‐4‐yl)amino]‐hexanoyl ceramide (C 6 ‐NBD‐cer). The kinetic parameters for C 6 ‐NBD‐cer were comparable to those for the synthetic substrate N ‐acetylsphinganine used previously. Aureobasidin A acted as a tight‐binding, non‐competitive inhibitor with respect to C 6 ‐NBD‐cer and had a K i of 0.55 nM." @default.
- W1973566996 created "2016-06-24" @default.
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- W1973566996 date "1999-12-17" @default.
- W1973566996 modified "2023-10-06" @default.
- W1973566996 title "Inhibition of yeast inositol phosphorylceramide synthase by aureobasidin A measured by a fluorometric assay" @default.
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- W1973566996 doi "https://doi.org/10.1016/s0014-5793(99)01633-6" @default.
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