Abstract
"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.
