1985 年 105 巻 5 号 p. 430-441
Esters of p-amidinophenol have been demonstrated to undergo efficient and specific tryptic hydrolysis. These esters are characterized by their linkage, i.e., the site specific groups for the enzyme (charged amidinium) is not involved in their carbonyl groups but in the leaving portion. Thus, these esters were named "inverse substrates" with respect to their structure and kinetic properties. It was also found that these esters were hydrolyzed by various proteases which show trypsin-like specificity. A facile procedure for the preparation of acyl-enzymes carrying non specific residue was described and the potential usefulness of the "inverse substrates" concept was proposed.