Poststatin, a new inhibitor of prolyl endopeptidase, produced by Streptomyces viridochromogenes MH534-30F3. II. Structure determination and inhibitory activities

J Antibiot (Tokyo). 1991 Sep;44(9):956-61. doi: 10.7164/antibiotics.44.956.

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

  • Amino Acid Sequence
  • Chemical Phenomena
  • Chemistry
  • Chromatography, High Pressure Liquid
  • Endopeptidases / metabolism*
  • Molecular Sequence Data
  • Oligopeptides / analysis
  • Oligopeptides / pharmacology*
  • Prolyl Oligopeptidases
  • Serine Endopeptidases*
  • Serine Proteinase Inhibitors / analysis
  • Serine Proteinase Inhibitors / pharmacology*
  • Streptomyces / chemistry*

Substances

  • Oligopeptides
  • Serine Proteinase Inhibitors
  • poststatin
  • Endopeptidases
  • Serine Endopeptidases
  • Prolyl Oligopeptidases