"Inverse substrates" for trypsin-like enzymes.
"Inverse substrates" for bovine thrombin and human plasmin were demonstrated. "Inverse substrates" for the enzymes are characterized as specific substrates in which the arrangement of site-specific group is reversed compared to that of normal substrate, e.g., a cationic center is included in their leaving group instead of being in their acyl moiety (K.Tanizawa, Y.Kasaba, Y.Kanaoka, J. Am. Chem. Soc. 99. 4485-4488). Kinetic characteristics of thrombin, plasmin and trypsin toward "inverse substrates" were compared. Based on these observations, differences in active centers of the trypsin homologs were discussed. Behavior of p- and m-hydroxyphenylguanidine derivatives as new "inverse substrates" for trypsin was also reported.
D000818:Animals; D001550:Benzamidines; D001665:Binding Sites; D002417:Cattle; D005341:Fibrinolysin / Q000378:metabolism*; D006146:Guanidines; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D013379:Substrate Specificity; D013917:Thrombin / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism*
D001550:Benzamidines; D006146:Guanidines; D014357:Trypsin; D013917:Thrombin; D005341:Fibrinolysin