Propeptin, a New Inhibitor of Prolyl Endopeptidase Produced by Microbispora: II. Determination of Chemical Structure

The structure of propeptin, a new inhibitor of prolyl endopeptidase isolated from Microbispora sp. SNA-115, was determined. FAB/MS, Edman degradation and amino acid analysis revealed propeptin to be a cyclic polypeptide consisting of 19 common L-amino acids. By FAB/MS and protein chemical methods, t...

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Veröffentlicht in:Journal of antibiotics 2002/03/25, Vol.55(3), pp.296-300
Hauptverfasser: ESUMI, YASUAKI, SUZUKI, YOSHIKATSU, ITOH, YUMIKO, URAMOTO, MASAKAZU, KIMURA, KEN-ICHI, GOTO, MASAAKI, YOSHIHAMA, MAKOTO, ICHIKAWA, TERUO
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Sprache:eng
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Zusammenfassung:The structure of propeptin, a new inhibitor of prolyl endopeptidase isolated from Microbispora sp. SNA-115, was determined. FAB/MS, Edman degradation and amino acid analysis revealed propeptin to be a cyclic polypeptide consisting of 19 common L-amino acids. By FAB/MS and protein chemical methods, the primary sequence of propeptin was determined to be Gly1-Tyr-Pro-Trp-Trp-Asp-Tyr-Arg-Asp9-Leu-Phe-Gly-Gly-His-Thr-Phe-Ile-Ser-Pro19, which cyclizes between the β-carboxyl group of Asp9 and the α-amino group of Gly1.
ISSN:0021-8820
1881-1469
DOI:10.7164/antibiotics.55.296