Eurystatins A and B, new prolyl endopeptidase inhibitors. II. Physico-chemical properties and structure determination.
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.
Toda
S
S
Bristol-Myers Squibb Research Institute, Tokyo, Japan.
Kotake
C
C
Tsuno
T
T
Narita
Y
Y
Yamasaki
T
T
Konishi
M
M
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
D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; C078927:eurystatin A; C078928:eurystatin B; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases