Inhibition of human leucocyte elastase by ursolic acid : evidence for a binding site for pentacyclic triterpenes

• Published in: Biochemical journal Vol. 277; no. 2; pp. 521 - 526
• Main Authors: QI-LONG YING, RINEHART, A. R, SIMON, S. R, CHERONIS, J. C
• Format: Journal Article
• Language: English
• Published: Colchester Portland Press 15.07.1991
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Anti-Infective Agents - pharmacology; Binding Sites; Biological and medical sciences; Elastin - metabolism; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; inhibition; Kinetics; leucocyte elastase; Leukocyte Elastase; man; Molecular Sequence Data; Molecular Structure; Oligopeptides - chemical synthesis; Pancreatic Elastase - antagonists & inhibitors; Substrate Specificity; Triterpenes - metabolism; Triterpenes - pharmacology; Ursolic Acid; Pentacyclic compound; Human; Radiolabelling; Enzyme; Triterpene; Elastase; Binding site; Inhibition; Kinetic parameter; Leucocyte elastase

Several pentacyclic triterpenoid metabolites of plant origin are inhibitors of hydrolysis of both synthetic peptide substrates and elastin by human leucocyte elastase (HLE). Ursolic acid, the most potent of these compounds, has an inhibition constant of 4-6 microM for hydrolysis of peptide substrate...