Propeptin, a new inhibitor of prolyl endopeptidase produced by Microbispora. I. Fermentation, isolation and biological properties.
Propeptin, an inhibitor of the prolyl endopeptidase isolated from the mycelium of Microbispora sp. SNA-115, is an atypical cyclic peptide antibiotic. It was purified by column chromatographies on silica gel and Sephadex LH-20 and high performance liquid chromatography using an ODS column. Propeptin has the molecular formula of C113H142N26O27 and consists of nineteen amino acids. Propeptin inhibited prolyl endopeptidase of the genus Flavobacterium competitively when Z-Gly-Pro-pNA was used as a substrate. The inhibitor constant (Ki) was 0.70 microM.
Kimura
K
K
Research Institute of Life Science, Snow Brand Milk Products Co., Ltd, Tochigi, Japan.
Kanou
F
F
Takahashi
H
H
Esumi
Y
Y
Uramoto
M
M
Yoshihama
M
M
D000192:Actinomycetales; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D002417:Cattle; D005285:Fermentation; D006801:Humans; D010456:Peptides, Cyclic / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; C107024:propeptin; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases