Inactivation of proteases and esterases by halomethylated derivatives of dihydrocoumarins.
A series of halomethylated derivatives of dihydrocoumarins has been found to inhibit irreversibly proteases and esterases. alpha-Chymotrypsin, subtilish, elastase are rapidly inactivated in the presence of these compounds, while trypsin, kallicrein, papain are inhibited more slowly. Esterases like acetylcholinesterase and butyrylcholinesterase also lose activity in their presence. Two structural features of these inactivators are essential for inhibition: a reactive cis-ester function and an alkylating function. Analogues of these derivatives having only one of these characteristics are inefficient. Therefore it is suggested that the efficiency of these bifunctional reagents is due to their character of potential "suicide substrates".
D002800:Cholinesterase Inhibitors; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D003374:Coumarins / Q000494:pharmacology*; D007610:Kallikreins / Q000037:antagonists & inhibitors; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D010206:Papain / Q000494:pharmacology; D011480:Protease Inhibitors; D013329:Structure-Activity Relationship; D013381:Subtilisins / Q000037:antagonists & inhibitors; D014361:Trypsin Inhibitors / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; D003374:Coumarins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D007610:Kallikreins; D013381:Subtilisins; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D010206:Papain