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J. Biochem, 1982, Vol. 91, No. 6 1837-1843
© 1982 Japanese Biochemical Society

research-article

Comparative Studies on the Structure of Active Sites. Behavior of "Inverse Substrates" toward Trypsin and Related Enzymes1

Masayuki NOZAWA, Faculty of Pharmaceutical Sciences2, Kazutaka TANIZAWA, Faculty of Pharmaceutical Sciences and Yuichi KANAOKA, Faculty of Pharmaceutical Sciences

Hokkaido University Kita-ku, Sapporo Hokkaido 060

The kinetics of hydrolysis of "inverse substrates," P-amidinophenyl alkanoates, catalyzed by urokinase, plasmin, kallikrein, and trypsins from various sources were studied. Dissociation constants of acyl enzyme-ligand complexes, which are a characteristic parameter of the reaction with "inverse substrates", were analyzed with a view to comparing the spatial requirements of active sites. It was concluded that the spatial restraint of the active site as regards coexistence of the acyl residue and specific ligand is strictest for hog pancreatic kallikrein and this restraint decreases in the following order: human urokinase; bovine plasmin, bovine and hog trypsins; Streptomyces fradiae trypsin; and Streptomyces griseus trypsin.

1Paper XVI in a series entitled Inverse Substrates. Paper XV; Fujioka, T., Tanizawa, K., and Kanaoka, Y. (1982) J. Pharm. Bull. 30, 230–236. This work was supported in part by grants from the Yamada Science Foundation, the Foundation for the Promotion of Medicinal Resources, and the Ministry of Education, Science and Culture of Japan.

2present address: Tokyo Research Laboratory, Dai-ichi Pure Chemicals Co., Ltd., Sumida-ku, Tokyo 130.


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