Abstract
Poststatin, a new inhibitor of prolyl endopeptidase, has been isolated from the culture broth of Streptomyces viridochromogenes MH534-30F3. The structure of poststatin was defined as L-valyl-L-valyl-3-amino-2-oxovaleryl-D-leucyl-L-valine by analysis of spectral properties and chemical studies of poststatin and its derivatives. The alpha-keto group of postine in poststatin plays the most important role on the inhibitory mechanism.
MeSH terms
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Amino Acid Sequence
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Chemical Phenomena
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Chemistry
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Chromatography, High Pressure Liquid
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Endopeptidases / metabolism*
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Molecular Sequence Data
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Oligopeptides / analysis
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Oligopeptides / pharmacology*
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Prolyl Oligopeptidases
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Serine Endopeptidases*
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Serine Proteinase Inhibitors / analysis
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Serine Proteinase Inhibitors / pharmacology*
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Streptomyces / chemistry*
Substances
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Oligopeptides
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Serine Proteinase Inhibitors
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poststatin
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Endopeptidases
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Serine Endopeptidases
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Prolyl Oligopeptidases