Specific inhibition of human granulocyte elastase with peptide aldehydes.
The kinetic features of human granulocyte elastase, chymotrypsin, porcine pancreatic elastase and elastomucoproteinase were compared. Amino acyl ester substrates were assayed and Km and kcat values were defined. Aldehyde analogues of the p-nitroanilide substrates designed for granulocyte elastase as optimal for Km appeared to be potent inhibitors. Suc-D-Phe-Pro-valinal (Ki = 40 microM) was found to inhibit granulocyte elastase competitively and specifically when measured with synthetic substrates, and the Ki was 3 microM with the natural protein substrate, elastin.
D000447:Aldehydes / Q000494:pharmacology*; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D010450:Endopeptidases; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000494:pharmacology*; D010179:Pancreas / Q000201:enzymology; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D000447:Aldehydes; D009842:Oligopeptides; D011480:Protease Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; C047138:elastomucoproteinase