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, 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 beta-carboxyl group of Asp9 and the a-amino group of Gly1.
Esumi
Yasuaki
Y
RIKEN (The Institute of Physical and Chemical Research), Saitama, Japan. esumi@postman.riken.go.jp
Suzuki
Yoshikatsu
Y
Itoh
Yumiko
Y
Uramoto
Masakazu
M
Kimura
Ken-ichi
K
Goto
Masaaki
M
Yoshihama
Makoto
M
Ichikawa
Teruo
T
D000192:Actinomycetales / Q000378:metabolism*; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; C107024:propeptin; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases