N,O-diacylhydroxylamines as enzyme-activated inhibitors for serine proteases.
Several N-peptidyl-O(4-nitrobenzoyl)-hydroxylamines were synthesized and their inhibitory action against dipeptidyl-peptidase IV, alpha-chymotrypsin, elastase and thermitase was investigated. If the petidyl residue can be recognized by the enzyme as a substrate, a time dependent irreversible inactivation occurs. The mechanism of inhibition by N,O-diacylhydroxylamines as enzyme activated inhibitors is discussed.
D000818:Animals; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors; D006898:Hydroxylamines / Q000138:chemical synthesis* / Q000494:pharmacology; D007700:Kinetics; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors / Q000138:chemical synthesis*; D012697:Serine Endopeptidases; D013552:Swine
D006898:Hydroxylamines; D011480:Protease Inhibitors; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D012697:Serine Endopeptidases; C022728:thermitase; D002918:Chymotrypsin; D010196:Pancreatic Elastase