文章基本信息

标题："INVERSE SUBSTRATES" FOR TRYPSIN-LIKE ENZYMES
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作者：MASAYUKI NOZAWA ; KAZUTAKA TANIZAWA ; YUICHI KANAOKA 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：1980
卷号：3
期号：4
页码：213-219
DOI：10.1248/bpb1978.3.213
出版社：The Pharmaceutical Society of Japan
摘要："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.
关键词：guanidinophenyl esters