Stable acyl-derivatives of trypsin-like enzymes. Preparation, kinetics, application.
Among the inhibitors with a benzamidine moiety, 4-amidinophenyl esters of aromatic carboxylic acids that possess the structure of "inverse substrates" exhibit special kinetic characteristics. These compounds behave like substrates of trypsin-like enzymes, but acylation is much more rapid than deacylation. The result is accumulation of a comparatively stable acyl-enzyme, which may be easily isolated. By the use of 4-amidinophenyl esters acyl-derivatives of various trypsin-like enzymes can be prepared. In vivo, an acyl-enzyme behaves as an inert form of the enzyme and is protected from being inactivated by inhibitors. It is slowly reactivated in the circulation and has stimulated growing interest as a potential pro-drug.
D000215:Acylation; D000818:Animals; D004793:Enzyme Reactivators / Q000138:chemical synthesis / Q000378:metabolism; D004795:Enzyme Stability; D006207:Half-Life; D007700:Kinetics; D014357:Trypsin / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000138:chemical synthesis / Q000378:metabolism
D004793:Enzyme Reactivators; D014361:Trypsin Inhibitors; D014357:Trypsin