Structure and Synthesis of E–64, a New Thiol Protease Inhibitor
- 1 March 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 42 (3) , 529-536
- https://doi.org/10.1080/00021369.1978.10863015
Abstract
E–64, a new thiol protease inhibitor, was isolated from a mold, as described previously.1) This was proved to consist of each one mole of L-leucine, agmatine and l-trans-epoxysuccinic acid by the analysis of the digestion products of E–64 by pronase. Moreover, the absolute structure of E–64 was assumed to be N-[N-(l-3-trans-carboxyoxiran-2-carbonyl)-l-leucyl]-agmatine and the identity was established by the comparison with its optical isomer which was obtained synthetically. The difference of optical activity of trans-epoxysuccinie acid gave no effect on papain Inhibitory activity.This publication has 1 reference indexed in Scilit:
- Derivatives of (-)-trans-2,3-Epoxysuccinic Acid and Some of their Biological EffectsJournal of Medicinal Chemistry, 1963