Inverse substrates: novel synthetic substrates for trypsin and related enzymes.
The kinetics of the reactions of trypsin and related enzymes with esters derived from p-amidinophenol have been studied. These esters were named "inverse substrates" with respect to their structure and kinetic characteristics. Preparation of a variety of acyltrypsins was carried out by use of these substrates. Spectral analysis of acyl trypsins carrying a reporter group provided valuable information on the microenvironments near the active site. Kinetic analysis of the behaviour of trypsin and related enzymes toward these novel-type substrates revealed characteristic function of the enzymes not manifested with typical substrates. These results were analyzed with a view to comparing the spatial requirements of the respective active site.
D000578:Amidines / Q000378:metabolism*; D000818:Animals; D001550:Benzamidines / Q000138:chemical synthesis / Q000378:metabolism*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007610:Kallikreins / Q000378:metabolism*; D013305:Streptomyces griseus; D013379:Substrate Specificity; D013552:Swine; D014357:Trypsin / Q000378:metabolism*; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D000578:Amidines; D001550:Benzamidines; D010450:Endopeptidases; D007610:Kallikreins; D014357:Trypsin; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator