title: Eurystatins A and B, new prolyl endopeptidase inhibitors. II. Physico-chemical properties and structure determination.
abstract: The structures of eurystatins A and B, new prolyl endopeptidase inhibitors, have been elucidated by chemical degradation and spectral studies. They have in common a unique 13-membered cyclic peptide core composed of L-leucine, L-ornithine and (S)-3-amino-2-oxobutyric acid, and differ from each other in the alpha,beta-unsaturated fatty acid attached to the alpha-amino moiety of the ornithine.
authors: Bristol-Myers Squibb Research Institute, Tokyo, Japan.
authors: S
authors: S
authors: Toda
authors: C
authors: C
authors: Kotake
authors: T
authors: T
authors: Tsuno
authors: Y
authors: Y
authors: Narita
authors: T
authors: T
authors: Yamasaki
authors: M
authors: M
authors: Konishi
mesh_terms: D005417:Flavobacterium / Q000187:drug effects / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000187:drug effects*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D013055:Spectrophotometry, Infrared; D013302:Streptomyces / Q000737:chemistry / Q000145:classification; D013329:Structure-Activity Relationship
chemical_list: D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; C078927:eurystatin A; C078928:eurystatin B; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases