Poststatin, a new inhibitor of prolyl endopeptidase, produced by Streptomyces viridochromogenes MH534-30F3. II. Structure determination and inhibitory activities.
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.
Institute of Microbial Chemistry, Tokyo, Japan.
M
M
Nagai
K
K
Ogawa
Y
Y
Muraoka
H
H
Naganawa
T
T
Aoyagi
T
T
Takeuchi
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis / Q000494:pharmacology*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors / Q000032:analysis / Q000494:pharmacology*; D013302:Streptomyces / Q000737:chemistry*
D009842:Oligopeptides; D015842:Serine Proteinase Inhibitors; C071400:poststatin; D010450:Endopeptidases; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases